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Database: UniProt
Entry: A0A0G1GI85_9BACT
LinkDB: A0A0G1GI85_9BACT
Original site: A0A0G1GI85_9BACT 
ID   A0A0G1GI85_9BACT        Unreviewed;       312 AA.
AC   A0A0G1GI85;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-SEP-2023, entry version 26.
DE   RecName: Full=aspartate carbamoyltransferase {ECO:0000256|ARBA:ARBA00013008};
DE            EC=2.1.3.2 {ECO:0000256|ARBA:ARBA00013008};
GN   Name=pyrB {ECO:0000313|EMBL:KKS98503.1};
GN   ORFNames=UV73_C0001G0024 {ECO:0000313|EMBL:KKS98503.1};
OS   Candidatus Gottesmanbacteria bacterium GW2011_GWA2_43_14.
OC   Bacteria; Candidatus Gottesmanbacteria.
OX   NCBI_TaxID=1618443 {ECO:0000313|EMBL:KKS98503.1, ECO:0000313|Proteomes:UP000034894};
RN   [1] {ECO:0000313|EMBL:KKS98503.1, ECO:0000313|Proteomes:UP000034894}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC         aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58228; EC=2.1.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001363};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004852}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. {ECO:0000256|RuleBase:RU003634}.
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:KKS98503.1}.
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DR   EMBL; LCFP01000001; KKS98503.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1GI85; -.
DR   STRING; 1618443.UV73_C0001G0024; -.
DR   PATRIC; fig|1618443.3.peg.24; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000034894; Unassembled WGS sequence.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR002082; Asp_carbamoyltransf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   NCBIfam; TIGR00670; asp_carb_tr; 1.
DR   PANTHER; PTHR45753:SF6; ASPARTATE CARBAMOYLTRANSFERASE; 1.
DR   PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00101; ATCASE.
DR   SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003634}.
FT   DOMAIN          8..149
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          156..308
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
SQ   SEQUENCE   312 AA;  34877 MW;  0747551F892EF4AF CRC64;
     MINSLFGKDL TTVDSLTSAD LELIWTKSGE MQEIVNRKKS DNRLQGKITA MLFFEPSTRT
     FSSFLTAVQR LGGGSLPFNG MKNTSVEKGE SFEHTIRVFS VYADCLIIRH PEIGYPARAA
     ALTDNPVINA GDGAGEHPSQ AVFDTYTILK RFPEKKELTV TLAGDLKYGR TVHSLSKLLL
     KCGRKITFNL VSPLMLSMPS QITEALERNS SVRRTDQLKE AVNGSDVIYM TRVQKERFND
     PDEYEKLKSF YRLNKSLLTG ANKEVIIMHP LPIAAGEISP EMDNDPRSLY LNEQLKNGLS
     VRMALLDLIL NP
//
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