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Protein

Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit

Gene

pyrK

Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD+.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterUniRule annotationNote: Binds 1 [2Fe-2S] cluster per subunit.UniRule annotation
  • FADUniRule annotationNote: Binds 1 FAD per subunit.UniRule annotation

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes orotate from (S)-dihydroorotate (NAD(+) route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit (pyrK)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes orotate from (S)-dihydroorotate (NAD(+) route), the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi211Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi216Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi219Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi231Iron-sulfur (2Fe-2S)UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi50 – 53FADUniRule annotation4
Nucleotide bindingi72 – 73FADUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Pyrimidine biosynthesis, Transport

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00070; UER00945.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunitUniRule annotation
Alternative name(s):
Dihydroorotate oxidase B, electron transfer subunitUniRule annotation
Gene namesi
Name:pyrKUniRule annotation
Ordered Locus Names:CA_C2651
OrganismiClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Taxonomic identifieri272562 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000000814 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001483581 – 246Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunitAdd BLAST246

Proteomic databases

PRIDEiQ97FS6.

Interactioni

Subunit structurei

Heterotetramer of 2 PyrK and 2 PyrD type B subunits.UniRule annotation

Protein-protein interaction databases

STRINGi272562.CA_C2651.

Structurei

3D structure databases

ProteinModelPortaliQ97FS6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 97FAD-binding FR-typeUniRule annotationAdd BLAST95

Sequence similaritiesi

Belongs to the PyrK family.UniRule annotation
Contains 1 FAD-binding FR-type domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DF0. Bacteria.
COG0543. LUCA.
HOGENOMiHOG000225118.
KOiK02823.
OMAiEEKMACG.

Family and domain databases

Gene3Di2.10.240.10. 1 hit.
HAMAPiMF_01211. DHODB_Fe_S_bind. 1 hit.
InterProiIPR012165. Cyt_c3_hydrogenase_gsu.
IPR019480. Dihydroorotate_DH_Fe-S-bd.
IPR023455. Dihydroorotate_DHASE_ETsu.
IPR017927. Fd_Rdtase_FAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF10418. DHODB_Fe-S_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF006816. Cyc3_hyd_g. 1 hit.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q97FS6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKEKYTVEKV YENIKVEDGI YKLSIKGEFE VRPGQFYLLR AWDIEPTLSR
60 70 80 90 100
PISIYDADDE KISFLYSVVG KGTEILSKLK SGDEIKITGP LGNGFNVKRI
110 120 130 140 150
SGKVAIVCGG IGVAPMVYLA KNLKNCNVDF YAGFKTVSKT VDNVEKYVKE
160 170 180 190 200
LKLSTEDGSI GHKGYVTDNF KPEEYDYVLC CGPEIMMYKV VKMCEQKNVP
210 220 230 240
VYISMEKKMA CGIGACLVCT CKTKGGRRRA CKEGPVFLGS ELILND
Length:246
Mass (Da):27,418
Last modified:October 1, 2001 - v1
Checksum:i641286714D951CB7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001437 Genomic DNA. Translation: AAK80598.1.
PIRiC97226.
RefSeqiNP_349258.1. NC_003030.1.
WP_010965939.1. NC_003030.1.

Genome annotation databases

EnsemblBacteriaiAAK80598; AAK80598; CA_C2651.
GeneIDi1118834.
KEGGicac:CA_C2651.
PATRICi32039667. VBICloAce74127_2840.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001437 Genomic DNA. Translation: AAK80598.1.
PIRiC97226.
RefSeqiNP_349258.1. NC_003030.1.
WP_010965939.1. NC_003030.1.

3D structure databases

ProteinModelPortaliQ97FS6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272562.CA_C2651.

Proteomic databases

PRIDEiQ97FS6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK80598; AAK80598; CA_C2651.
GeneIDi1118834.
KEGGicac:CA_C2651.
PATRICi32039667. VBICloAce74127_2840.

Phylogenomic databases

eggNOGiENOG4105DF0. Bacteria.
COG0543. LUCA.
HOGENOMiHOG000225118.
KOiK02823.
OMAiEEKMACG.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00945.

Family and domain databases

Gene3Di2.10.240.10. 1 hit.
HAMAPiMF_01211. DHODB_Fe_S_bind. 1 hit.
InterProiIPR012165. Cyt_c3_hydrogenase_gsu.
IPR019480. Dihydroorotate_DH_Fe-S-bd.
IPR023455. Dihydroorotate_DHASE_ETsu.
IPR017927. Fd_Rdtase_FAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF10418. DHODB_Fe-S_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF006816. Cyc3_hyd_g. 1 hit.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPYRK_CLOAB
AccessioniPrimary (citable) accession number: Q97FS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: October 1, 2001
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.