B4U8P2 (B4U8P2_HYDS0) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Dihydroorotase HAMAP MF_00220
Short name=DHOase HAMAP MF_00220
EC=3.5.2.3 HAMAP MF_00220

Gene names

Name:	pyrC HAMAP MF_00220
Ordered Locus Names:	HY04AAS1_0816

Organism

Hydrogenobaculum sp. (strain Y04AAS1) [Complete proteome] [HAMAP]

Taxonomic identifier

380749 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Hydrogenobaculum

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00220 RuleBase RU003441 SAAS SAAS002195
Cofactor	Binds 2 zinc ions per subunit By similarity. HAMAP MF_00220 RuleBase RU003441 SAAS SAAS002195
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00220 RuleBase RU003441 SAAS SAAS002195
Subunit structure	Homodimer By similarity. HAMAP MF_00220 SAAS SAAS002195
Sequence similarities	Belongs to the DHOase family. Type 2 subfamily. HAMAP MF_00220 RuleBase RU003441

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis HAMAP MF_00220 RuleBase RU003441 SAAS SAAS002195
Ligand	Metal-binding HAMAP MF_00220 RuleBase RU003441 SAAS SAAS002195 Zinc HAMAP MF_00220 SAAS SAAS002195 RuleBase RU003441
Molecular function	Hydrolase HAMAP MF_00220 RuleBase RU003441 SAAS SAAS002195 EMBL ACG57503.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	dihydroorotase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Metal binding	62	1	Zinc 1 By similarity HAMAP MF_00220
	Metal binding	64	1	Zinc 1 By similarity HAMAP MF_00220
	Metal binding	144	1	Zinc 1; via carbamate group By similarity HAMAP MF_00220
	Metal binding	144	1	Zinc 2; via carbamate group By similarity HAMAP MF_00220
	Metal binding	181	1	Zinc 2 By similarity HAMAP MF_00220
	Metal binding	234	1	Zinc 2 By similarity HAMAP MF_00220
	Metal binding	307	1	Zinc 1 By similarity HAMAP MF_00220
Amino acid modifications
	Modified residue	144	1	N6-carboxylysine By similarity HAMAP MF_00220

Sequences

	Sequence		Length	Mass (Da)
	B4U8P2 [UniParc]. Last modified September 23, 2008. Version 1. Checksum: 6343DC004F3F6B8E	FASTA	424	46,908
	10 20 30 40 50 60 MSRNLLIKSA RLIEPNLNFD KEVDILIKDD KIDKISEYID KKDYNTVEAK GLIACSGFVD 70 80 90 100 110 120 IHAHLRDPGF TYKEDLESGM KAATFGGFTT IVCMPNTNPP IDNESIISYI LSKAEKIGIC 130 140 150 160 170 180 DVKVSACVTK NRSGKELTDF YRLKKAGTVC FTDDGSPVQD QKLMLKALEM VSLLNSFVAN 190 200 210 220 230 240 HCEDDAFAGN GAFDEGAFSS VYGLPFRPSY AEDVMVARDC ILSYKTGGKL HIQHLSSSLS 250 260 270 280 290 300 VDIVKFFKEK GANITCEVNP NHLALNSFAA FKKKTILKVN PPIRDYKTQE ALIKALQEGV 310 320 330 340 350 360 IDCIATDHAP HAKNEKLHPI KGAAGMLGFQ VALPIIMSLV KDGVIDIKSL ITLMSKNPAK 370 380 390 400 410 420 ILGFDNTIKE GALANLVLWH PSHEWLFDES INPSKSSNSP FLNSVLTSKV FYTIYKGNIV YRYY

References

[1]

"Complete and draft genome sequences of six members of the Aquificales." Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A. J. Bacteriol. 191:1992-1993(2009) [PubMed: 19136599] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001130 Genomic DNA. Translation: ACG57503.1.
RefSeq	YP_002121481.1. NC_011126.1.
3D structure databases
ProteinModelPortal	B4U8P2.
ModBase	Search...
Protein-protein interaction databases
STRING	B4U8P2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6743622.
GenomeReviews	Gene locus HY04AAS1_0816 in contig CP001130_GR.
KEGG	hya:HY04AAS1_0816.
PATRIC	22136308. VBIHydSp64203_0822.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG724623.
OMA	CDVHPVG.
Family and domain databases
HAMAP	MF_00220_B. PyrC_type2_B. [Tree]
InterPro	IPR006680. Amidohydro_1. IPR004722. DHOase. IPR002195. Dihydroorotase_CS. IPR011059. Metal-dep_hydrolase_composite. [Graphical view]
KO	K01465.
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
SUPFAM	SSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMs	TIGR00857. PyrC_multi. 1 hit.
PROSITE	PS00482. DIHYDROOROTASE_1. 1 hit. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

B4U8P2_HYDS0

Accession

Primary (citable) accession number: B4U8P2

Entry history

Integrated into UniProtKB/TrEMBL:	September 23, 2008
Last sequence update:	September 23, 2008
Last modified:	December 14, 2011
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)