NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
"Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium caulinodans ORS571.";
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.

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 .
SIMILARITY: Belongs to the ATCase/OTCase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AP009384; BAF88849.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001525767.1; -.

3D structure databases

ModBase

A8ICW0.

Ontologies

GO:0004070;	Molecular function: aspartate carbamoyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0006221;	Biological process: pyrimidine nucleotide biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00001; -; 1.
PBIL [Tree]

InterPro

IPR006130; Asp/Orn_carbamoyltranf.
IPR006132; Asp/Orn_carbamoyltranf_P_bd.
IPR006131; Asp_carbamoyltransf_Asp/Orn_bd.
IPR002082; Aspartate_carbamoyltransf_euk.
Graphical view of domain structure.

Pfam

PF00185; OTCace; 1.
PF02729; OTCace_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00100; AOTCASE.
PR00101; ATCASE.

TIGRFAMs

TIGR00670; asp_carb_tr; 1.

PROSITE

PS00097; CARBAMOYLTRANSFERASE; 1.

BLOCKS

A8ICW0.

Genome annotation databases

GeneID

5689256; -.

GenomeReviews

AP009384_GR; AZC_2851.

CMR

A8ICW0; AZC_2851.

Other

ProtoNet

A8ICW0.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Pyrimidine biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 321`	`321`		`Aspartate carbamoyltransferase.`	`PRO_0000321072`

Sequence information

Length: 321 AA [This is the length of the unprocessed precursor]

Molecular weight: 34923 Da [This is the MW of the unprocessed precursor]

CRC64: 2E66C91ACBAAACCB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MITAPFFTLD RRDLLGIEGL SAPEIVGLLD LAEEFVVLNR QIEKKRSTLR GRTQVNLFFE 

        70         80         90        100        110        120 
ASTRTQSSFE LAGKRLGADV MNMSVGNSSV KKGETLIDTA MTLNAMRPDI LVVRHHASGA 

       130        140        150        160        170        180 
VALLARKVDC CVVNAGDGAH EHPTQALLDA LTIRRNKGRI EGLTVAVCGD VLHSRVARSN 

       190        200        210        220        230        240 
ILLLHTLGAR VRVVAPSTLL PTGIENFGVE VHRSMESGLE GADIVMMLRL QRERMAGSFI 

       250        260        270        280        290        300 
PSVKEYFHYY GLDEAKLKRA KPDALVMHPG PMNRGVEIDS AVADGAQSLI REQVEMGVAV 

       310        320 
RMAVLDALAR KLPNATGAER D

A8ICW0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools