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Database: UniProt
Entry: Q8VKU2_PSEAI
LinkDB: Q8VKU2_PSEAI
Original site: Q8VKU2_PSEAI 
ID   Q8VKU2_PSEAI            Unreviewed;       208 AA.
AC   Q8VKU2;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=carbamoyl-phosphate synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012738};
DE            EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
DE   Flags: Fragment;
GN   Name=carA {ECO:0000313|EMBL:CAC88814.1};
OS   Pseudomonas aeruginosa.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287 {ECO:0000313|EMBL:CAC88814.1};
RN   [1] {ECO:0000313|EMBL:CAC88814.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ICMP 8647 {ECO:0000313|EMBL:CAC88814.1};
RX   PubMed=15103237; DOI=10.1023/B:ANTO.0000024910.57117.16;
RA   Hilario E., Buckley T.R., Young J.M.;
RT   "Improved resolution on the phylogenetic relationships among Pseudomonas by
RT   the combined analysis of atp D, car A, rec A and 16S rDNA.";
RL   Antonie Van Leeuwenhoek 86:51-64(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001777};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004812}.
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DR   EMBL; AJ414208; CAC88814.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8VKU2; -.
DR   MEROPS; C26.954; -.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00099; CPSGATASE.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT   DOMAIN          1..84
FT                   /note="Carbamoyl-phosphate synthase small subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01097"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAC88814.1"
FT   NON_TER         208
FT                   /evidence="ECO:0000313|EMBL:CAC88814.1"
SQ   SEQUENCE   208 AA;  22720 MW;  700B363199519620 CRC64;
     QQIVTLTYPH IGNTGTTPED AEANRVWAAG LIIRDLPLIA SNWRSKQSLP DYLKANGTVA
     IAGIDTRRLT RILREKGSQN GCILAGADAT EERALELARA FPGLKGMDLA KEVTTAERYE
     WRSSVWNLES DSHPEIPAGE LPYHVVAYDY GVKLNILRML VARGCRLTVV PAQTPASEVL
     ALNPDGIFLS NGPGDPEPCD YAIQAIRE
//
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