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Protein

Aspartate carbamoyltransferase

Gene

pyrB

Organism
Clostridium botulinum (strain Eklund 17B / Type B)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.UniRule annotation

Pathway: UMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase (glutamine-hydrolyzing) (CB17B0060), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA)
  2. Aspartate carbamoyltransferase (pyrB), Aspartate carbamoyltransferase (pyrB)
  3. Dihydroorotase (pyrC), Dihydroorotase (pyrC)
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 (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Enzyme and pathway databases

BioCyciCBOT508765:GJ4H-2570-MONOMER.
UniPathwayiUPA00070; UER00116.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate carbamoyltransferaseUniRule annotation (EC:2.1.3.2UniRule annotation)
Alternative name(s):
Aspartate transcarbamylaseUniRule annotation
Short name:
ATCaseUniRule annotation
Gene namesi
Name:pyrBUniRule annotation
Ordered Locus Names:CLL_A2581
OrganismiClostridium botulinum (strain Eklund 17B / Type B)
Taxonomic identifieri935198 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000001195 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 307307Aspartate carbamoyltransferasePRO_1000088750Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB2TNG3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATCase/OTCase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0540.
HOGENOMiHOG000022685.
OMAiYGVPVRM.
OrthoDBiEOG61KBJZ.

Family and domain databases

Gene3Di3.40.50.1370. 2 hits.
HAMAPiMF_00001. Asp_carb_tr.
InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
[Graphical view]
PfamiPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSiPR00100. AOTCASE.
PR00101. ATCASE.
SUPFAMiSSF53671. SSF53671. 1 hit.
TIGRFAMsiTIGR00670. asp_carb_tr. 1 hit.
PROSITEiPS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2TNG3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKDKHLIDP MDFTVEELEE IFKLAHEIIL DPEKFSHVCE GKILGTLFYE
60 70 80 90 100
PSTRTRFSFE AAMMRLGGKI LGFSEPNSSS ASKGESLSDT IKMVSIYTDI
110 120 130 140 150
IAMRHPKEGS AKVASLYSSV PIINAGDGGH QHPTQTLTDL LTIEMLKDGL
160 170 180 190 200
SNHTIGICGD LKYGRTVHSL IKAMSRYKGN KFLLISPKEL RIPDYIREEI
210 220 230 240 250
LRKNNIEFLE VETLEEVIDK VDILYMTRIQ KERFFNEEEY LRLRDSYILN
260 270 280 290 300
KEKMNLAKSD MIVMHPLPRV NEIACEVDYD KRAAYFKQAE YGMYARMALM

AKLLGVL
Length:307
Mass (Da):35,157
Last modified:July 1, 2008 - v1
Checksum:i373E089ACECEF97E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001056 Genomic DNA. Translation: ACD24851.1.
RefSeqiWP_012425577.1. NC_010674.1.
YP_001886770.1. NC_010674.1.

Genome annotation databases

EnsemblBacteriaiACD24851; ACD24851; CLL_A2581.
GeneIDi19963415.
PATRICi19397980. VBICloBot123574_2495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001056 Genomic DNA. Translation: ACD24851.1.
RefSeqiWP_012425577.1. NC_010674.1.
YP_001886770.1. NC_010674.1.

3D structure databases

ProteinModelPortaliB2TNG3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACD24851; ACD24851; CLL_A2581.
GeneIDi19963415.
PATRICi19397980. VBICloBot123574_2495.

Phylogenomic databases

eggNOGiCOG0540.
HOGENOMiHOG000022685.
OMAiYGVPVRM.
OrthoDBiEOG61KBJZ.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00116.
BioCyciCBOT508765:GJ4H-2570-MONOMER.

Family and domain databases

Gene3Di3.40.50.1370. 2 hits.
HAMAPiMF_00001. Asp_carb_tr.
InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
[Graphical view]
PfamiPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSiPR00100. AOTCASE.
PR00101. ATCASE.
SUPFAMiSSF53671. SSF53671. 1 hit.
TIGRFAMsiTIGR00670. asp_carb_tr. 1 hit.
PROSITEiPS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of Clostridium botulinum strain Eklund."
    Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
    Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Eklund 17B / Type B.

Entry informationi

Entry nameiPYRB_CLOBB
AccessioniPrimary (citable) accession number: B2TNG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: June 24, 2015
This is version 51 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

External Data

Dasty 3

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 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.