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Protein

Carbamoyl-phosphate synthase small chain

Gene

carA

Organism
Lactobacillus plantarum subsp. plantarum ATCC 14917 = JCM 1149 = CGMCC 1.2437
Status
Unreviewed-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), Carbamoyl-phosphate synthase small chain (carA), 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), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB)
  2. Aspartate carbamoyltransferase (pyrB)
  3. 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei241NucleophileUniRule annotation1
Active sitei326UniRule annotation1
Active sitei328UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigaseUniRule annotationImported
Biological processAmino-acid biosynthesis, Arginine biosynthesisUniRule annotation, Pyrimidine biosynthesisUniRule annotation
LigandATP-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

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 annotationImported
ORF Names:HMPREF0531_12321Imported
OrganismiLactobacillus plantarum subsp. plantarum ATCC 14917 = JCM 1149 = CGMCC 1.2437Imported
Taxonomic identifieri525338 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
Proteomesi
  • UP000005567 Componenti: Unassembled WGS sequence

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

ProteinModelPortaliD7VDU8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 167CPSaseUniRule annotationAdd BLAST167

Sequence similaritiesi

Belongs to the CarA family.UniRule annotation

Keywords - Domaini

Glutamine amidotransferaseUniRule annotation

Phylogenomic databases

OrthoDBiPOG091H01NP.

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.
IPR036480. CarbP_synth_ssu_N_sf.
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.

D7VDU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKYLTLADG TQWIGTAIGD CQLEVAGRIV FNTGMTGYQE TLTDPSYLNQ
60 70 80 90 100
MIAFTYPLIG NYGIDPTVAQ APTIGAQAII VHELTTFNDH YTSRQSLASF
110 120 130 140 150
LTIHHVAGIE GVDTRDLTIH IRQTGAQMAI LSNHPITDFE AQLATFAPQV
160 170 180 190 200
LTATPLPVAT TTIRPRVAIL NFGEKAAITA ELQARGADIV VLPPTASLKA
210 220 230 240 250
VAAYHPDGIL LSNGPGDPTD YHTYLATIRQ LAQRYPLAGI CLGHQLIALA
260 270 280 290 300
YGAQTYQLSF GHHGLNHPVQ ACADGRIIMT SQNHDYAVDP ASIKGTPLIV
310 320 330 340 350
THTELNDGSI EGLRLPHQAV MSVQFHPEAH PGPQEAGQFF DDFLLTIQKE

AVVNA
Length:355
Mass (Da):38,259
Last modified:October 5, 2010 - v1
Checksum:iEFE8140D23368063
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ACGZ02000027 Genomic DNA. Translation: EFK28643.1.
RefSeqiWP_003642068.1. NZ_GL379763.1.

Genome annotation databases

EnsemblBacteriaiEFK28643; EFK28643; HMPREF0531_12321.
PATRICifig|525338.16.peg.958.

Similar proteinsi

Entry informationi

Entry nameiD7VDU8_LACPN
AccessioniPrimary (citable) accession number: D7VDU8
Entry historyiIntegrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: October 25, 2017
This is version 46 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Keywords - Technical termi

Complete proteomeImported