Reviewed, UniProtKB/Swiss-Prot Q5P6I4 (PYRB_AZOSE)

Names and origin

Protein names

Recommended name:
    Aspartate carbamoyltransferase
    EC=2.1.3.2
Alternative name(s):
    Aspartate transcarbamylase
      Short name=ATCase

Gene names

Name:	pyrB
Ordered Locus Names:	AZOSEA09520
ORF Names:	ebA1759

Organism

Azoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)) [Complete proteome] [HAMAP]

Taxonomic identifier

76114 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 2/6.
Sequence similarities	Belongs to the ATCase/OTCase family.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro amino acid metabolic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	amino acid binding Inferred from electronic annotation. Source: InterPro aspartate carbamoyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 323	323	Aspartate carbamoyltransferase		PRO_0000113088

Sequences

	Sequence		Length	Mass (Da)
	Q5P6I4-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 5901B825CE352FBA	FASTA	323	35,268
	10 20 30 40 50 60 MRNPQLNKHG ELQHLLTIDG LPRSILTAIL DTAAPFTEVA EREVKKLPLL RGKSIFNLFF 70 80 90 100 110 120 ENSTRTRTTF EIAAKRLSAD VVNLNVSTSS AAKGESLLDT VDNLSAMQAD MFVVRHAASG 130 140 150 160 170 180 APFLIAQHLF ATGRDHIHVV NAGDGRHAHP TQGLLDMYTI RHFKRDFTNL TIAIVGDVLH 190 200 210 220 230 240 SRVARSQIGA LTTLGVPEVR VIGPKTLLPT DVERLGVRVF HDIREGLRGV DVVMMLRLQN 250 260 270 280 290 300 ERMNGALLPT PQEFYKVWGL TAEKLALAKP DAIVMHPGPM NRGVEIDSSV ADGAQAVILP 310 320 QVTFGIAVRM AVMSMLAGQQ GSK

References

[1]	"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1." Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R. Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR555306 Genomic DNA. Translation: CAI07077.1.
RefSeq	YP_157978.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3180228.
GenomeReviews	Gene locus AZOSEA09520 in contig CR555306_GR.
KEGG	eba:ebA1759.
NMPDR	fig|76114.4.peg.393.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5P6I4.
Enzyme and pathway databases
BioCyc	ASP76114:EBA1759-MON.
Family and domain databases
HAMAP	MF_00001. [Tree]
InterPro	IPR006130. Asp/Orn_carbamoyltranf. IPR006132. Asp/Orn_carbamoyltranf_P_bd. IPR006131. Asp_carbamoyltransf_Asp/Orn_bd. IPR002082. Aspartate_carbamoyltransf_euk. [Graphical view]
Pfam	PF00185. OTCace. 1 hit. PF02729. OTCace_N. 1 hit. [Graphical view]
PRINTS	PR00100. AOTCASE. PR00101. ATCASE.
TIGRFAMs	TIGR00670. asp_carb_tr. 1 hit.
PROSITE	PS00097. CARBAMOYLTRANSFERASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRB_AZOSE

Accession

Primary (citable) accession number: Q5P6I4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	January 4, 2005
Last modified:	November 25, 2008
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)