ID H2DQW0_PSEFL Unreviewed; 205 AA.
AC H2DQW0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:AEY79707.1};
OS Pseudomonas fluorescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294 {ECO:0000313|EMBL:AEY79707.1};
RN [1] {ECO:0000313|EMBL:AEY79707.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=K7 {ECO:0000313|EMBL:AEY79707.1};
RX PubMed=23510642; DOI=10.1016/j.micres.2013.02.006;
RA Viggor S., Juhanson J., Joesaar M., Mitt M., Truu J., Vedler E.,
RA Heinaru A.;
RT "Dynamic changes in the structure of microbial communities in Baltic Sea
RT coastal seawater microcosms modified by crude oil, shale oil or diesel
RT fuel.";
RL Microbiol. Res. 168:415-427(2013).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR EMBL; JN642672; AEY79707.1; -; Genomic_DNA.
DR AlphaFoldDB; H2DQW0; -.
DR MEROPS; C26.954; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
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:AEY79707.1"
FT NON_TER 205
FT /evidence="ECO:0000313|EMBL:AEY79707.1"
SQ SEQUENCE 205 AA; 22294 MW; AE8BD0E04B61EC22 CRC64;
QQIVTLTYPH IGNTGTTPED VESDCVWSAG LVIRDLPLVA SNWRNTMSLS DYLKANNVVA
IAGIDTRRLT RILREKGSQN GCIMVGDNIS EEAAIAAAQG FPGLKGMDLA KVVSAKEKYE
WRSTVWDLKT DSHATIEAAD LPYHVVAYDY GVKYNILRML VERGCRVTVV PAQTPASEVL
ALQPDGVFLS NGPGDPEPCD YAIQA
//
