ID A0A1G1MP77_9BACT Unreviewed; 359 AA.
AC A0A1G1MP77;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=carbamoyl-phosphate synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012738};
DE EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
GN ORFNames=A3K83_02695 {ECO:0000313|EMBL:OGX19247.1};
OS Omnitrophica WOR_2 bacterium RBG_13_44_8b.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801836 {ECO:0000313|EMBL:OGX19247.1, ECO:0000313|Proteomes:UP000177397};
RN [1] {ECO:0000313|EMBL:OGX19247.1, ECO:0000313|Proteomes:UP000177397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC -!- SIMILARITY: Belongs to the CarA family.
CC {ECO:0000256|ARBA:ARBA00007800}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGX19247.1}.
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DR EMBL; MHGJ01000024; OGX19247.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1MP77; -.
DR Proteomes; UP000177397; Unassembled WGS sequence.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
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 NCBIfam; TIGR01368; CPSaseIIsmall; 1.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 1..131
FT /note="Carbamoyl-phosphate synthase small subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01097"
SQ SEQUENCE 359 AA; 39028 MW; E1A38E1D9741CAF0 CRC64;
MKAILMLEDG KNFVGESLGI QGEAIGELIF NTAVVGYQEM ITDPANSGKI LVLTYPLIGN
YGVAPKFNES KGVWPSGLIF KEKSRIVSNW QAKDSLDNFV KIHKLLTITG VDTRTLAVHL
RQKGSMLGIV STKTSDAKEL LSRIESFRNR GAQSILPKIS VTKAKTLGPK RAKLKIAILD
LGIQNSLIKQ LETLGLYMTV LPYNTPAEQI LGLKPQGLII SGGPEDDIGL KDVAANVKKL
IGQIPILGIS AGHEVLAAAL GAKVIKMKLG HHGVNYPIQY PASYKGEITV QNHSYVVDAG
SLNKIRDVKI IGFNLNDRTV EEIESRKLKL LGVQYIPASP GFAEVNSALK KFIKIIKKE
//
