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Database: UniProt
Entry: Q3LTU6_PSEME
LinkDB: Q3LTU6_PSEME
Original site: Q3LTU6_PSEME 
ID   Q3LTU6_PSEME            Unreviewed;       205 AA.
AC   Q3LTU6;
DT   25-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 43.
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:ABA26634.1};
OS   Pseudomonas mendocina.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=300 {ECO:0000313|EMBL:ABA26634.1};
RN   [1] {ECO:0000313|EMBL:ABA26634.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PC12 {ECO:0000313|EMBL:ABA26634.1};
RX   PubMed=16906406; DOI=10.1007/s00203-006-0143-3;
RA   Merimaa M., Heinaru E., Liivak M., Vedler E., Heinaru A.;
RT   "Grouping of phenol hydroxylase and catechol 2,3-dioxygenase genes among
RT   phenol- and p-cresol-degrading Pseudomonas species and biotypes.";
RL   Arch. Microbiol. 186:287-296(2006).
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; DQ178192; ABA26634.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3LTU6; -.
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:ABA26634.1"
FT   NON_TER         205
FT                   /evidence="ECO:0000313|EMBL:ABA26634.1"
SQ   SEQUENCE   205 AA;  22575 MW;  C7287EFA5BCAC1B3 CRC64;
     QQIVTLTYPH IGNTGTTPED AESNRVWAAG LIIRDLPLIS SNWRDKQPLD EYLKANGTVA
     IAGIDTRRLT RILREKGSQN GCILVGDDAT EEKALELARS FPGLKGMDLA KVVSCTERYE
     WRESTWNLQS DSHPEIPASE LPYHVVAYDY GVKLNILRML VERGCRLTVV PAQTPASDVL
     ALNPDGVFLS NGPGDPEPCD YAIQA
//
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