StarFunc result for job id P26440

User Input

>input (426 residues)
MAEMATATRLLGWRVASWRLRPPLAGFVSQRAHSLLPVDDAINGLSEEQRQLRQTMAKFL
QEHLAPKAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISR
ASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMK
LKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTS
KKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQA
VLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDC
AGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRA
FNADFH

Proteins with similar structure

Top structural analogs (as identified by Foldseek and TM-align)

Rank	Structure template	TM-score1	TM-score2	Foldseek E-value	Length	ID1	ID2	Download	Description
1	AFDB:P26440	1.000	1.000	2.775E-67	426	1.000	1.000	P26440.pdb.gz	IVD_HUMAN Isovaleryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=IVD PE=1 SV=2
2	AFDB:P12007	0.969	0.974	1.043E-61	424	0.894	0.899	P12007.pdb.gz	IVD_RAT Isovaleryl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus OX=10116 GN=Ivd PE=1 SV=2
3	PDB:1ivhA	0.904	0.995	7.617E-59	387	0.906	0.997	1ivhA.pdb.gz	Structure of human isovaleryl-CoA dehydrogenase at 2.6 A resolution: structural basis for substrate specificity,.
4	AFDB:G5EEH6	0.914	0.929	8.896E-51	419	0.631	0.642	G5EEH6.pdb.gz	G5EEH6_CAEEL Isovaleryl-CoA dehydrogenase, mitochondrial OS=Caenorhabditis elegans OX=6239 GN=ivd-1 PE=1 SV=1
5	AFDB:Q9SWG0	0.885	0.921	5.321E-47	409	0.606	0.631	Q9SWG0.pdb.gz	IVD_ARATH Isovaleryl-CoA dehydrogenase, mitochondrial OS=Arabidopsis thaliana OX=3702 GN=IVD PE=1 SV=2
6	AFDB:Q9FS87	0.878	0.908	1.533E-46	412	0.599	0.619	Q9FS87.pdb.gz	IVD_SOLTU Isovaleryl-CoA dehydrogenase, mitochondrial OS=Solanum tuberosum OX=4113 GN=IVD PE=1 SV=2
7	AFDB:Q9FS88	0.904	0.934	1.930E-46	412	0.582	0.602	Q9FS88.pdb.gz	MBCD_SOLTU 2-methylacyl-CoA dehydrogenase, mitochondrial OS=Solanum tuberosum OX=4113 GN=2MBCD PE=1 SV=2
8	AFDB:Q9I296	0.880	0.968	1.216E-45	387	0.563	0.620	Q9I296.pdb.gz	Q9I296_PSEAE Isovaleryl-CoA dehydrogenase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=liuA PE=3 SV=1
9	AFDB:G3KIM8	0.863	0.932	3.127E-34	394	0.347	0.376	G3KIM8.pdb.gz	ACRC_ANAPI Acryloyl-CoA reductase (NADH) OS=Anaerotignum propionicum OX=28446 GN=acrC PE=1 SV=1
10	AFDB:Q3ZBF6	0.891	0.921	9.878E-34	412	0.333	0.345	Q3ZBF6.pdb.gz	ACADS_BOVIN Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus OX=9913 GN=ACADS PE=1 SV=1
11	AFDB:E5KSD5	0.904	0.934	1.427E-33	412	0.343	0.354	E5KSD5.pdb.gz	E5KSD5_HUMAN Acyl-Coenzyme A dehydrogenase, C-2 to C-3 short chain OS=Homo sapiens OX=9606 GN=ACADS PE=3 SV=1
12	PDB:1jqiA	0.872	0.966	9.541E-33	384	0.326	0.362	1jqiA.pdb.gz	Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases.
13	PDB:1rx0A	0.856	0.948	6.281E-31	384	0.282	0.312	1rx0A.pdb.gz	Structures of Isobutyryl-CoA Dehydrogenase and Enzyme-Product Complex: COMPARISON WITH ISOVALERYL- AND SHORT-CHAIN ACYL-COA DEHYDROGENASES.
14	PDB:2a1tC	0.865	0.949	7.875E-29	388	0.296	0.325	2a1tC.pdb.gz	Stabilization of Non-productive Conformations Underpins Rapid Electron Transfer to Electron-transferring Flavoprotein
15	PDB:6af6A	0.847	0.940	2.728E-28	383	0.284	0.316	6af6A.pdb.gz	Crystal Structure of PigA: A Prolyl Thioester-Oxidizing Enzyme in Prodigiosin Biosynthesis.
16	PDB:6fahC	0.854	0.958	8.230E-28	379	0.315	0.354	6fahC.pdb.gz	Molecular basis of the flavin-based electron-bifurcating caffeyl-CoA reductase reaction.
17	PDB:7s7gA	0.820	0.618	8.214E-27	571	0.296	0.221	7s7gA.pdb.gz	Crystal Structure Analysis of Human VLCAD
18	PDB:2r0mA	0.835	0.911	1.491E-25	390	0.258	0.282	2r0mA.pdb.gz	The effect of a Glu370Asp mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate.
19	PDB:2ix6A	0.867	0.887	4.499E-25	416	0.258	0.264	2ix6A.pdb.gz	Controlling Electron Transfer in Acyl-Coa Oxidases and Dehydrogenases: A Structural View.
20	PDB:4xvxB	0.779	0.885	1.775E-20	373	0.195	0.223	4xvxB.pdb.gz	A covalent adduct of MbtN, an acyl-ACP dehydrogenase from Mycobacterium tuberculosis, reveals an unusual acyl-binding pocket.

(a)	The query structure is shown in cartoon, while the structural analog is displayed using a backbone trace.
(b)	Ranking of proteins is based on E-value of Foldseek alignment.
(c)	TM-score1 and ID1 are TM-score and sequence identity normalized by query sequence length.
(d)	TM-score2 and ID2 are TM-score and sequence identity normalized by template sequence length.

Proteins with similar sequence

Top sequence homologs in UniProt

Rank	Template	E-value	Bit-score	Length	ID1	ID2	Description
1	A0A0A0MT83	0.0	878	423	0.993	1.000	A0A0A0MT83_HUMAN Isovaleryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=IVD PE=1 SV=2
2	G5EEH6	0.0	552	419	0.620	0.630	G5EEH6_CAEEL Isovaleryl-CoA dehydrogenase, mitochondrial OS=Caenorhabditis elegans OX=6239 GN=ivd-1 PE=1 SV=1
3	P12007	0.0	800	424	0.899	0.903	IVD_RAT Isovaleryl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus OX=10116 GN=Ivd PE=1 SV=2
4	P26440	0.0	885	426	1.000	1.000	IVD_HUMAN Isovaleryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=IVD PE=1 SV=2
5	Q9FS87	0.0	514	412	0.582	0.602	IVD_SOLTU Isovaleryl-CoA dehydrogenase, mitochondrial OS=Solanum tuberosum OX=4113 GN=IVD PE=1 SV=2
6	Q9FS88	0.0	523	412	0.582	0.602	MBCD_SOLTU 2-methylacyl-CoA dehydrogenase, mitochondrial OS=Solanum tuberosum OX=4113 GN=2MBCD PE=1 SV=2
7	Q9JHI5	0.0	797	424	0.894	0.899	IVD_MOUSE Isovaleryl-CoA dehydrogenase, mitochondrial OS=Mus musculus OX=10090 GN=Ivd PE=1 SV=1
8	Q9SWG0	1.64e-179	508	409	0.592	0.616	IVD_ARATH Isovaleryl-CoA dehydrogenase, mitochondrial OS=Arabidopsis thaliana OX=3702 GN=IVD PE=1 SV=2
9	Q9I296	6.61e-176	498	387	0.563	0.620	Q9I296_PSEAE Isovaleryl-CoA dehydrogenase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=liuA PE=3 SV=1
10	H0YN10	4.94e-130	375	212	0.430	0.863	H0YN10_HUMAN Isovaleryl-CoA dehydrogenase (Fragment) OS=Homo sapiens OX=9606 GN=IVD PE=1 SV=1
11	Q387A0	1.84e-85	268	411	0.338	0.350	Q387A0_TRYB2 Isovaleryl-coA dehydrogenase, putative OS=Trypanosoma brucei brucei (strain 927/4 GUTat10.1) OX=185431 GN=Tb11.55.0026 PE=3 SV=1
12	Q07417	4.03e-85	268	412	0.331	0.342	ACADS_MOUSE Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus OX=10090 GN=Acads PE=1 SV=2
13	P15651	9.63e-84	264	412	0.326	0.337	ACADS_RAT Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus OX=10116 GN=Acads PE=1 SV=2
14	E5KSD5	1.51e-83	263	412	0.333	0.345	E5KSD5_HUMAN Acyl-Coenzyme A dehydrogenase, C-2 to C-3 short chain OS=Homo sapiens OX=9606 GN=ACADS PE=3 SV=1
15	P16219	1.51e-83	263	412	0.333	0.345	ACADS_HUMAN Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=ACADS PE=1 SV=1
16	G3KIM8	4.63e-82	259	394	0.347	0.376	ACRC_ANAPI Acryloyl-CoA reductase (NADH) OS=Anaerotignum propionicum OX=28446 GN=acrC PE=1 SV=1
17	Q9DBL1	1.02e-81	259	432	0.331	0.326	ACDSB_MOUSE Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus OX=10090 GN=Acadsb PE=1 SV=1
18	Q95U46	9.22e-80	254	414	0.322	0.331	Q95U46_DROME GH07925p OS=Drosophila melanogaster OX=7227 GN=CG3902 PE=2 SV=1
19	Q9VVU1	1.30e-79	253	414	0.322	0.331	Q9VVU1_DROME FI09602p OS=Drosophila melanogaster OX=7227 GN=GH07925p PE=1 SV=1
20	A0A0S2Z3P9	3.72e-79	253	432	0.326	0.322	A0A0S2Z3P9_HUMAN Acyl-CoA dehydrogenase short/branched chain isoform 1 (Fragment) OS=Homo sapiens OX=9606 GN=ACADSB PE=2 SV=1

(a)	Ranking of proteins is based on the E-value of a BLASTp alignment.
(b)	ID1 and ID2 are sequence identities normalized by the query and template sequence lengths, respectively.

Pfam families

Top Pfam family matches

Rank	Pfam family	E-value	Score	Description
1	PF00441 Acyl-CoA_dh_1	5.8e-35	132.2	Acyl-CoA dehydrogenase, C-terminal domain
2	PF08028 Acyl-CoA_dh_2	1.5e-05	36.7	Acyl-CoA dehydrogenase, C-terminal domain
3	PF02770 Acyl-CoA_dh_M	5.4e-24	95.5	Acyl-CoA dehydrogenase, middle domain
4	PF02771 Acyl-CoA_dh_N	9.4e-35	131.0	Acyl-CoA dehydrogenase, N-terminal domain

(a)	Ranking of Pfam families is based on the E-value provided by HMMsearch.

Protein-protein interaction (PPI) partners

Top PPI partners to 9606.ENSP00000418397

Rank	PPI partner	STRING score	Description
1	9606.ENSP00000343657	0.993	Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
2	9606.ENSP00000265594	0.981	Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
3	9606.ENSP00000318351	0.977	2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
4	9606.ENSP00000359151	0.976	Dihydrolipoamide branched chain transacylase E2
5	9606.ENSP00000269980	0.969	2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
6	9606.ENSP00000357535	0.962	Enoyl-CoA hydratase, mitochondrial
7	9606.ENSP00000231887	0.949	Peroxisomal bifunctional enzyme
8	9606.ENSP00000370023	0.944	Trifunctional enzyme subunit alpha, mitochondrial
9	9606.ENSP00000205402	0.929	Dihydrolipoyl dehydrogenase, mitochondrial
10	9606.ENSP00000419027	0.853	This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites . Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl- CoA/(S)-methylmalonyl-CoA . Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxy [...]
11	9606.ENSP00000426638	0.852	Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
12	9606.ENSP00000452762	0.843	Electron transfer flavoprotein subunit alpha, mitochondrial
13	9606.ENSP00000346173	0.823	Electron transfer flavoprotein subunit beta
14	9606.ENSP00000265395	0.813	3-hydroxyisobutyrate dehydrogenase, mitochondrial
15	9606.ENSP00000365462	0.790	This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites . Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl- CoA/(S)-methylmalonyl-CoA (PubMed:8434582, PubMed:6765947, PubMed:10101253). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, [...]
16	9606.ENSP00000364883	0.739	Methylglutaconyl-CoA hydratase, mitochondrial
17	9606.ENSP00000352706	0.727	3-hydroxyisobutyryl-CoA hydrolase, mitochondrial
18	9606.ENSP00000255189	0.707	Dimethylglycine dehydrogenase, mitochondrial
19	9606.ENSP00000356015	0.661	Acetyl-CoA acetyltransferase, cytosolic
20	9606.ENSP00000283871	0.658	Homogentisate 1,2-dioxygenase

A higher STRING score indicates a greater likelihood of interaction.
The query and PPI partners are shown as grey oval and white rectangles, respectively.
Interactions between query and PPI partners are shown by solid black lines. Interactions among PPI partners are by dashed grey lines.
Values in the rectangles are the STRING scores between query and each corresponding PPI partner

Predicted Gene Ontology (GO) Terms

GO term	C-score	Name
GO:0003995	1.000	acyl-CoA dehydrogenase activity
GO:0005515	0.996	protein binding
GO:0097159	0.817	organic cyclic compound binding
GO:1901363	0.804	heterocyclic compound binding
GO:0043167	0.597	ion binding
GO:0036094	0.520	small molecule binding
GO:0000166	0.424	nucleotide binding
GO:0043168	0.396	anion binding

C-score is the confidence score of a predicted GO term. Its value ranges from (0,1], where a higher value indicates a higher confidence prediction.
If a child GO term and its parent term have the same C-score, only the child term is shown in this table.

The graph shows the predicted terms for the Molecular Function (MF) GO aspect. GO terms shown in the table are colored by C-score in the graph:

[0.3,0.4)

[0.4,0.5)

[0.5,0.6)

[0.6,0.7)

[0.7,0.8)

[0.8,0.9)

[0.9,1.0]

GO term	C-score	Name
GO:0046395	0.997	carboxylic acid catabolic process
GO:1901564	0.996	organonitrogen compound metabolic process
GO:0016042	0.996	lipid catabolic process
GO:0032787	0.996	monocarboxylic acid metabolic process
GO:0030258	0.995	lipid modification
GO:0009081	0.992	branched-chain amino acid metabolic process
GO:0044242	0.986	cellular lipid catabolic process
GO:0006631	0.985	fatty acid metabolic process
GO:0009062	0.982	fatty acid catabolic process
GO:0019395	0.981	fatty acid oxidation
GO:0009063	0.981	amino acid catabolic process
GO:0009083	0.973	branched-chain amino acid catabolic process
GO:1901606	0.969	alpha-amino acid catabolic process
GO:0006635	0.968	fatty acid beta-oxidation
GO:0006551	0.850	leucine metabolic process

C-score is the confidence score of a predicted GO term. Its value ranges from (0,1], where a higher value indicates a higher confidence prediction.
If a child GO term and its parent term have the same C-score, only the child term is shown in this table.

The graph shows the predicted terms for the Biological Process (BP) GO aspect. GO terms shown in the table are colored by C-score in the graph:

[0.3,0.4)

[0.4,0.5)

[0.5,0.6)

[0.6,0.7)

[0.7,0.8)

[0.8,0.9)

[0.9,1.0]

GO term	C-score	Name
GO:0070013	1.000	intracellular organelle lumen
GO:0005739	1.000	mitochondrion
GO:0005634	0.973	nucleus
GO:0031981	0.935	nuclear lumen
GO:0005654	0.922	nucleoplasm
GO:0005759	0.896	mitochondrial matrix

C-score is the confidence score of a predicted GO term. Its value ranges from (0,1], where a higher value indicates a higher confidence prediction.
If a child GO term and its parent term have the same C-score, only the child term is shown in this table.

The graph shows the predicted terms for the Cellular Component (CC) GO aspect. GO terms shown in the table are colored by C-score in the graph:

[0.3,0.4)

[0.4,0.5)

[0.5,0.6)

[0.6,0.7)

[0.7,0.8)

[0.8,0.9)

[0.9,1.0]

Predicted reactions (EC numbers and Rhea reactions)

Reaction	C-score	Name
EC:1.3.-.-	1.000	Acting on the CH-CH group of donors.

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