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Protein

Carbamoyl-phosphate synthase small chain

Gene

carA

Organism
Neisseria gonorrhoeae
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. no protein annotated in this organism
  3. no protein annotated in this organism
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei266 – 2661NucleophileUniRule annotation
Active sitei350 – 3501UniRule annotation
Active sitei352 – 3521UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, 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 annotation
OrganismiNeisseria gonorrhoeae
Taxonomic identifieri485 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Carbamoyl-phosphate synthase small chainPRO_0000112297Add
BLAST

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.

Protein-protein interaction databases

STRINGi528357.NgonPI_010100001412.

Structurei

3D structure databases

ProteinModelPortaliQ50983.
SMRiQ50983. Positions 5-368.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini190 – 377188Glutamine amidotransferase type-1UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 186186CPSaseAdd
BLAST

Sequence similaritiesi

Belongs to the CarA family.UniRule annotation
Contains 1 glutamine amidotransferase type-1 domain.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4105C1M. Bacteria.
COG0505. LUCA.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_01209. CPSase_S_chain.
InterProiIPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
[Graphical view]
PfamiPF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SMARTiSM01097. CPSase_sm_chain. 1 hit.
[Graphical view]
SUPFAMiSSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01368. CPSaseIIsmall. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q50983-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTPALLVLA DGSVFHGTSI GYEGSASGEV VFNTSMTGYQ EILTDPSYCK
60 70 80 90 100
QIVTLTYPHI GNTGTNAEDE ESRSVYAAGL IIRDLPLLHS NFRASESLHD
110 120 130 140 150
YLVRNETVAI ADIDTRRLTM LLREKGAQGG AILTGADATV EKAQELIAAF
160 170 180 190 200
GSMVGKDLAK EVSCTETYEW TEGEWELGKG FVTPDKQPYH VVAYDFGVKT
210 220 230 240 250
NILRMLASRG CRLTVVPAQT SAEDVLALNP DGVFLSNGPG DPEPCTYGIE
260 270 280 290 300
AVQKLMESGK PIFGICLGHQ LISLAIGAKT LKMRFSHHGA NHPVQDLDSG
310 320 330 340 350
KVVITSQNHG FAVDADTLPA NARITHKSLF DNTLQGIELT DKPVSCFQGH
360 370
PEASPGPQDV GYLSDKFIGN MKAAKQA
Length:377
Mass (Da):40,515
Last modified:November 1, 1996 - v1
Checksum:iBD54FAF60506BCA2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631T → A in AAA74995 (PubMed:7773412).Curated
Sequence conflicti74 – 774SVYA → TVLP in AAA74995 (PubMed:7773412).Curated
Sequence conflicti127 – 1271Missing in AAA74995 (PubMed:7773412).Curated
Sequence conflicti205 – 2084MLAS → ISP in AAA74995 (PubMed:7773412).Curated
Sequence conflicti237 – 2382NG → QR in AAA74995 (PubMed:7773412).Curated
Sequence conflicti248 – 2481G → A in AAA74995 (PubMed:7773412).Curated
Sequence conflicti345 – 3451S → F in AAA74995 (PubMed:7773412).Curated
Sequence conflicti364 – 3641S → F in AAA74995 (PubMed:7773412).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54242 Genomic DNA. Translation: CAA91011.1.
U11295 Genomic DNA. Translation: AAA74995.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54242 Genomic DNA. Translation: CAA91011.1.
U11295 Genomic DNA. Translation: AAA74995.1.

3D structure databases

ProteinModelPortaliQ50983.
SMRiQ50983. Positions 5-368.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi528357.NgonPI_010100001412.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C1M. Bacteria.
COG0505. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_01209. CPSase_S_chain.
InterProiIPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
[Graphical view]
PfamiPF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SMARTiSM01097. CPSase_sm_chain. 1 hit.
[Graphical view]
SUPFAMiSSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01368. CPSaseIIsmall. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The Neisseria gonorrhoae carA gene: generation of mutants and implication of pyrimidine biosynthesis for the infection of epithelial cells."
    Rudel T., Boxberger H.J., Pandit J., Meyer T.F.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MS11.
  2. "Organization of carbamoyl-phosphate synthase genes in Neisseria gonorrhoeae includes a large, variable intergenic sequence which is also present in other Neisseria species."
    Lawson F.S., Billowes F.M., Dillon J.A.
    Microbiology 141:1183-1191(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CH811.

Entry informationi

Entry nameiCARA_NEIGO
AccessioniPrimary (citable) accession number: Q50983
Secondary accession number(s): Q59598
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.