NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
Submitted (DEC-2006) 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

CP000512; ABM31508.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_969282.1; -.

3D structure databases

ModBase

A1TKM0.

Ontologies

GO:0016597;	Molecular function: amino acid binding (inferred from electronic annotation from InterPro).
GO:0004070;	Molecular function: aspartate carbamoyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0006207;	Biological process: 'de novo' pyrimidine base biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006520;	Biological process: amino acid metabolic process (inferred from electronic annotation from InterPro).
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.

ProtoNet

A1TKM0.

Genome annotation databases

GeneID

4666793; -.

GenomeReviews

CP000512_GR; Aave_0910.

KEGG

aav:Aave_0910; -.

NMPDR

fig|397945.5.peg.790; -.

CMR

A1TKM0; Aave_0910.

Other

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`	`1 320`	`320`		`Aspartate carbamoyltransferase.`	`PRO_0000321062`

Sequence information

Length: 320 AA [This is the length of the unprocessed precursor]

Molecular weight: 34841 Da [This is the MW of the unprocessed precursor]

CRC64: 3DE6D497A3A42AFB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSKRNPQLN RNGELIHLLS IEGLPRSIVT HILDTAANFV SVNDREVKKV PLLRGKSVFN 

        70         80         90        100        110        120 
LFFENSTRTR TTFEIAAKRL SADVLNLDIA RSSASKGESL LDTIANLSAM AADLFVVRHS 

       130        140        150        160        170        180 
ESGAPYLIAQ HVAPHVHVIN AGDGRHAHPT QGLLDMYTIR HYKKDFSNLT VAIVGDVLHS 

       190        200        210        220        230        240 
RVARSDIHGL TTLGCPEVRV VGPRTLVPGD LSHMGVRVCH TLEEGIRDAD VVIMLRLQNE 

       250        260        270        280        290        300 
RMSGALLPSS QEYFKSFGLT PEKLRLAKPD AIVMHPGPIN RGVEIDSAVV DGPQAVILPQ 

       310        320 
VTFGIAVRMA VMSIVAGNEA

A1TKM0 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