StarFunc result for job id Q02127

User Input

>input (395 residues)
MAWRHLKKRAQDAVIILGGGGLLFASYLMATGDERFYAEHLMPTLQGLLDPESAHRLAVR
FTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSV
TPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVN
LGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQER
DGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSET
GGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTF
WGPPVVGKVKRELEALLKEQGFGGVTDAIGADHRR

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:Q02127	1.000	1.000	1.064E-82	395	1.000	1.000	Q02127.pdb.gz	PYRD_HUMAN Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Homo sapiens OX=9606 GN=DHODH PE=1 SV=3
2	AFDB:O35435	0.998	0.998	1.081E-76	395	0.876	0.876	O35435.pdb.gz	PYRD_MOUSE Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Mus musculus OX=10090 GN=Dhodh PE=1 SV=2
3	PDB:6et4A	0.918	0.987	1.010E-70	367	0.929	1.000	6et4A.pdb.gz	A DHODH inhibitor increases p53 synthesis and enhances tumor cell killing by p53 degradation blockage.
4	PDB:4oriA	0.890	0.990	2.033E-62	355	0.800	0.890	4oriA.pdb.gz	Fluorine Modulates Species Selectivity in the Triazolopyrimidine Class of Plasmodium falciparum Dihydroorotate Dehydrogenase Inhibitors.
5	AFDB:P32746	0.880	0.758	1.324E-51	460	0.514	0.441	P32746.pdb.gz	PYRD_ARATH Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Arabidopsis thaliana OX=3702 GN=PYRD PE=1 SV=2
6	AFDB:P32748	0.903	0.881	2.233E-51	405	0.486	0.474	P32748.pdb.gz	PYRD_DROME Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Drosophila melanogaster OX=7227 GN=Dhod PE=2 SV=2
7	AFDB:P32747	0.879	0.786	8.570E-48	443	0.463	0.413	P32747.pdb.gz	PYRD_SCHPO Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ura3 PE=1 SV=1
8	AFDB:Q874I4	0.896	0.800	1.043E-46	444	0.456	0.405	Q874I4.pdb.gz	PYRD_CANAL Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=URA9 PE=1 SV=1
9	AFDB:Q08210	0.897	0.632	7.754E-42	569	0.367	0.255	Q08210.pdb.gz	PYRD_PLAF7 Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Plasmodium falciparum (isolate 3D7) OX=36329 GN=PFF0160c PE=1 SV=1
10	AFDB:P9WHL1	0.816	0.901	8.284E-39	357	0.380	0.420	P9WHL1.pdb.gz	PYRD_MYCTU Dihydroorotate dehydrogenase (quinone) OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=pyrD PE=1 SV=1
11	AFDB:P0A7E1	0.777	0.910	1.514E-37	336	0.349	0.411	P0A7E1.pdb.gz	PYRD_ECOLI Dihydroorotate dehydrogenase (quinone) OS=Escherichia coli (strain K12) OX=83333 GN=pyrD PE=1 SV=1
12	PDB:1f76A	0.776	0.908	2.402E-36	336	0.344	0.405	1f76A.pdb.gz	E. coli Dihydroorotate Dehydrogenase Reveals Structural and Functional Distinction between different classes of dihydroorotate dehydrogenases
13	AFDB:G5EB61	0.837	0.642	3.493E-36	520	0.370	0.281	G5EB61.pdb.gz	G5EB61_EMENI Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=ANIA_05909 PE=3 SV=1
14	PDB:4xq6B	0.722	0.887	1.206E-33	320	0.352	0.434	4xq6B.pdb.gz	Crystal structure of Dihydroorotate Dehydrogenase form Mycobacterium Tuberculosis
15	PDB:5xfwD	0.652	0.809	8.786E-22	315	0.218	0.273	5xfwD.pdb.gz
16	PDB:4ef8B	0.652	0.810	1.320E-21	314	0.200	0.252	4ef8B.pdb.gz	Target sites for the design of anti-trypanosomatid drugs based on the structure of dihydroorotate dehydrogenase.
17	PDB:1ep3A	0.653	0.816	1.159E-19	311	0.215	0.273	1ep3A.pdb.gz	Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster.
18	PDB:1gthA	0.636	0.258	6.772E-18	1019	0.170	0.066	1gthA.pdb.gz	Crystal structure of the productive ternary complex of dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil. Implications for mechanism of inhibition and electron transfer.
19	PDB:3sgzA	0.464	0.535	1.333E-10	336	0.149	0.176	3sgzA.pdb.gz	High resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1, 2, 3-thiadiazole. Implications for inhibitor specificity and drug design.
20	PDB:7r4pA	0.460	0.529	9.074E-10	337	0.129	0.151	7r4pA.pdb.gz	Structure of human hydroxyacid oxidase 1 bound with 5-bromo-N-methyl-1H-indazole-3-carboxamide

(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	I3NI32	0.0	783	393	0.995	1.000	I3NI32_HUMAN Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Homo sapiens OX=9606 GN=DHODH PE=1 SV=1
2	O35435	0.0	702	395	0.876	0.876	PYRD_MOUSE Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Mus musculus OX=10090 GN=Dhodh PE=1 SV=2
3	Q02127	0.0	791	395	1.000	1.000	PYRD_HUMAN Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Homo sapiens OX=9606 GN=DHODH PE=1 SV=3
4	Q63707	0.0	703	395	0.886	0.886	PYRD_RAT Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Rattus norvegicus OX=10116 GN=Dhodh PE=1 SV=1
5	P32746	8.95e-127	375	460	0.537	0.461	PYRD_ARATH Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Arabidopsis thaliana OX=3702 GN=PYRD PE=1 SV=2
6	I3L449	2.27e-122	353	193	0.430	0.881	I3L449_HUMAN Dihydroorotate dehydrogenase (quinone) (Fragment) OS=Homo sapiens OX=9606 GN=DHODH PE=1 SV=1
7	P32748	1.39e-121	360	405	0.476	0.464	PYRD_DROME Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Drosophila melanogaster OX=7227 GN=Dhod PE=2 SV=2
8	P32747	4.69e-106	321	443	0.446	0.397	PYRD_SCHPO Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ura3 PE=1 SV=1
9	Q874I4	1.26e-103	315	444	0.435	0.387	PYRD_CANAL Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=URA9 PE=1 SV=1
10	J3QRQ3	1.05e-101	299	144	0.365	1.000	J3QRQ3_HUMAN Dihydroorotate dehydrogenase (quinone) (Fragment) OS=Homo sapiens OX=9606 GN=DHODH PE=1 SV=1
11	Q08210	4.87e-82	263	569	0.380	0.264	PYRD_PLAF7 Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Plasmodium falciparum (isolate 3D7) OX=36329 GN=PFF0160c PE=1 SV=1
12	P0A7E1	4.43e-73	233	336	0.365	0.429	PYRD_ECOLI Dihydroorotate dehydrogenase (quinone) OS=Escherichia coli (strain K12) OX=83333 GN=pyrD PE=1 SV=1
13	P9WHL1	7.05e-73	233	357	0.367	0.406	PYRD_MYCTU Dihydroorotate dehydrogenase (quinone) OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=pyrD PE=1 SV=1
14	G5EB61	4.40e-50	178	520	0.375	0.285	G5EB61_EMENI Dihydroorotate dehydrogenase (quinone), mitochondrial OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=ANIA_05909 PE=3 SV=1
15	P54322	1.14e-20	93.6	311	0.230	0.293	PYRDB_LACLM Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit OS=Lactococcus lactis subsp. cremoris (strain MG1363) OX=416870 GN=pyrDB PE=1 SV=2
16	Q57U83	3.24e-15	78.2	313	0.213	0.268	PYRD_TRYB2 Dihydroorotate dehydrogenase (fumarate) OS=Trypanosoma brucei brucei (strain 927/4 GUTat10.1) OX=185431 GN=Tb927.5.3830 PE=1 SV=1
17	Q725V9	1.24e-13	73.2	307	0.220	0.283	Q725V9_DESVH Dihydroorotate dehydrogenase OS=Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough) OX=882 GN=pyrD PE=1 SV=1
18	Q4QEW7	7.23e-13	71.2	320	0.220	0.272	Q4QEW7_LEIMA Dihydroorotate dehydrogenase (fumarate) OS=Leishmania major OX=5664 GN=DHODH PE=1 SV=1
19	P28272	1.40e-11	67.4	314	0.187	0.236	PYRD_YEAST Dihydroorotate dehydrogenase (fumarate) OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=URA1 PE=1 SV=1
20	Q95U76	7.40e-11	66.2	864	0.230	0.105	Q95U76_DROME Dihydropyrimidine dehydrogenase [NADP(+)] OS=Drosophila melanogaster OX=7227 GN=su(r) 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	PF01180 DHO_dh	7.8e-111	381.6	Dihydroorotate dehydrogenase
2	PF01070 FMN_dh	19	15.7	FMN-dependent dehydrogenase
3	PF03060 NMO	5.3e+02	11.4	Nitronate monooxygenase
4	PF03793 PASTA	63	14.9	PASTA domain
5	PF00290 Trp_syntA	1e+02	13.2	Tryptophan synthase alpha chain

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

Protein-protein interaction (PPI) partners

Top PPI partners to 9606.ENSP00000219240

Rank	PPI partner	STRING score	Description
1	9606.ENSP00000232607	0.995	Uridine 5'-monophosphate synthase
2	9606.ENSP00000264705	0.981	CAD protein
3	9606.ENSP00000419851	0.857	GMP synthase [glutamine-hydrolyzing]
4	9606.ENSP00000364320	0.844	mRNA turnover protein 4 homolog
5	9606.ENSP00000371253	0.837	Trifunctional purine biosynthetic protein adenosine-3
6	9606.ENSP00000253237	0.825	Glutamate-rich WD repeat-containing protein 1
7	9606.ENSP00000387365	0.818	Periodic tryptophan protein 1 homolog
8	9606.ENSP00000396308	0.815	Dihydrofolate reductase
9	9606.ENSP00000338862	0.808	Ribosome biogenesis protein BRX1 homolog
10	9606.ENSP00000361465	0.807	DNA-directed RNA polymerases I and III subunit RPAC1
11	9606.ENSP00000361704	0.803	CTP synthase 1
12	9606.ENSP00000322396	0.796	Ribosome biogenesis regulatory protein homolog
13	9606.ENSP00000371858	0.776	Probable 28S rRNA (cytosine(4447)-C(5))-methyltransferase
14	9606.ENSP00000416515	0.728	NADPH:adrenodoxin oxidoreductase, mitochondrial
15	9606.ENSP00000324343	0.714	Beta-ureidopropionase
16	9606.ENSP00000315774	0.712	NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
17	9606.ENSP00000381220	0.709	HD domain containing 2
18	9606.ENSP00000464317	0.707	Myosin-3
19	9606.ENSP00000263657	0.705	RNA-binding protein PNO1
20	9606.ENSP00000350698	0.686	Probable ATP-dependent RNA helicase DDX47

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:0004152	0.999	dihydroorotate dehydrogenase activity
GO:0005515	0.995	protein binding
GO:1901363	0.544	heterocyclic compound binding
GO:0097159	0.544	organic cyclic compound 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:0071704	0.995	organic substance metabolic process
GO:0044238	0.995	primary metabolic process
GO:0044237	0.995	cellular metabolic process
GO:0072528	0.987	pyrimidine-containing compound biosynthetic process
GO:0006725	0.981	cellular aromatic compound metabolic process
GO:0044281	0.950	small molecule metabolic process
GO:0019693	0.941	ribose phosphate metabolic process
GO:0009259	0.926	ribonucleotide metabolic process
GO:0006220	0.907	pyrimidine nucleotide metabolic process
GO:0019438	0.893	aromatic compound biosynthetic process
GO:0034654	0.867	nucleobase-containing compound biosynthetic process
GO:0009218	0.779	pyrimidine ribonucleotide metabolic process
GO:0090407	0.617	organophosphate biosynthetic process
GO:0009165	0.528	nucleotide biosynthetic process
GO:1901137	0.515	carbohydrate derivative biosynthetic process
GO:0065007	0.464	biological regulation
GO:0046390	0.433	ribose phosphate biosynthetic process
GO:0050789	0.428	regulation of biological process
GO:0050794	0.390	regulation of cellular process
GO:0009260	0.384	ribonucleotide biosynthetic process
GO:0006221	0.366	pyrimidine nucleotide biosynthetic 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:0005739	0.999	mitochondrion
GO:0070013	0.998	intracellular organelle lumen
GO:0005829	0.989	cytosol
GO:0005654	0.975	nucleoplasm
GO:0016020	0.902	membrane
GO:0005740	0.685	mitochondrial envelope
GO:0031090	0.569	organelle membrane
GO:0031966	0.542	mitochondrial membrane
GO:0005743	0.531	mitochondrial inner membrane

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
RHEA:18073	0.999	(S)-dihydroorotate + A = AH2 + orotate

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