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Protein

Carbamoyl-phosphate synthase small chain

Gene

carA

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.UniRule annotation

Pathwayi: L-arginine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes carbamoyl phosphate from bicarbonate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes carbamoyl phosphate from bicarbonate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1 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 small chain (carA), Carbamoyl-phosphate synthase large chain (carB)
  2. Aspartate carbamoyltransferase (pyrB)
  3. Dihydroorotase (ZMO1689)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei264NucleophileUniRule annotation1
Active sitei348UniRule annotation1
Active sitei350UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processAmino-acid biosynthesis, Arginine biosynthesis, Pyrimidine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

Protein family/group databases

MEROPSiC26.954.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase small chainUniRule annotation (EC:6.3.5.5UniRule annotation)
Alternative name(s):
Carbamoyl-phosphate synthetase glutamine chainUniRule annotation
Gene namesi
Name:carAUniRule annotation
Ordered Locus Names:ZMO1618
OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Taxonomic identifieri264203 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
Proteomesi
  • UP000001173 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001123541 – 374Carbamoyl-phosphate synthase small chainAdd BLAST374

Proteomic databases

PRIDEiO50235.

Interactioni

Subunit structurei

Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliO50235.
SMRiO50235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini187 – 374Glutamine amidotransferase type-1UniRule annotationAdd BLAST188

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 183CPSaseAdd BLAST183

Sequence similaritiesi

Belongs to the CarA family.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

HOGENOMiHOG000038087.
KOiK01956.

Family and domain databases

CDDicd01744. GATase1_CPSase. 1 hit.
Gene3Di3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_01209. CPSase_S_chain. 1 hit.
InterProiView protein in InterPro
IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR029062. Class_I_gatase-like.
IPR035686. CPSase_GATase1.
IPR017926. GATASE.
PfamiView protein in Pfam
PF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
SMARTiView protein in SMART
SM01097. CPSase_sm_chain. 1 hit.
SUPFAMiSSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01368. CPSaseIIsmall. 1 hit.
PROSITEiView protein in PROSITE
PS51273. GATASE_TYPE_1. 1 hit.

Sequencei

Sequence statusi: Complete.

O50235-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLADGQMIW GRGFGATGAK VGEVCFHTAM TGYEEIMTDP SFASQIINFT
60 70 80 90 100
FPHIGNVGAN REDVEAKTLH ALGCIVREDV TAPSNFRSLW RFDSWLKDHD
110 120 130 140 150
RIGLAGVDTR ALTGLLRKKG AQNAVIAHDP KGQFDIPALI ETARSWAGLQ
160 170 180 190 200
GMDLARSVST HQSYNWQEGI WSLQNGYSVV DNQKGPHVVA IDYGLKHNIL
210 220 230 240 250
RNLVEAGARV TVVKATASFD EVMAHKPDGV FLSNGPGDPA ATAEYAVPVI
260 270 280 290 300
RQLLDIKMPI FGICLGHQLL ALAVGATTYK MHQGHRGANH PVKRLDDSKV
310 320 330 340 350
EITSMNHGFA VATDSLPEQA RPTHLSLFDG SLAGLELTDR PAFSVQYHPE
360 370
ASPGPQDSYY LFTKFIDLIA KERP
Length:374
Mass (Da):40,808
Last modified:July 11, 2002 - v2
Checksum:i4C6BFA63818FE09E
GO

Sequence cautioni

The sequence AAC70355 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAV90242 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF086791 Genomic DNA. Translation: AAC70355.1. Different initiation.
AE008692 Genomic DNA. Translation: AAV90242.1. Different initiation.
PIRiT33716.

Genome annotation databases

EnsemblBacteriaiAAV90242; AAV90242; ZMO1618.
KEGGizmo:ZMO1618.

Similar proteinsi

Entry informationi

Entry nameiCARA_ZYMMO
AccessioniPrimary (citable) accession number: O50235
Secondary accession number(s): Q5NM18
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: July 11, 2002
Last modified: August 30, 2017
This is version 117 of the entry and version 2 of the sequence. See 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