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Database: UniProt
Entry: A0A0F9Z4Y7_9BACT
LinkDB: A0A0F9Z4Y7_9BACT
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ID   A0A0F9Z4Y7_9BACT        Unreviewed;       322 AA.
AC   A0A0F9Z4Y7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
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:KKP38824.1};
GN   ORFNames=UR28_C0012G0003 {ECO:0000313|EMBL:KKP38824.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWF2_33_10.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619065 {ECO:0000313|EMBL:KKP38824.1, ECO:0000313|Proteomes:UP000034183};
RN   [1] {ECO:0000313|EMBL:KKP38824.1, ECO:0000313|Proteomes:UP000034183}
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:KKP38824.1}.
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DR   EMBL; LBOP01000012; KKP38824.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F9Z4Y7; -.
DR   PATRIC; fig|1619065.3.peg.604; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000034183; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003634}.
FT   DOMAIN          6..157
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          171..317
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
FT   COILED          19..46
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   322 AA;  36841 MW;  7C30C35BBC436BCA CRC64;
     MKLPFQHLLK ASQFDPSLLK ILFDEARELE LRTKSLELRV KNSELRIENF GDGKILATVF
     WEPSTRTRFS FETAMLKLGG KVISNYSMET SSSITKGETL YDTAKTISSF ADIIAMRHPK
     EGAVAEFAKG SSVPVINAGD GSGDHPTQAL LDIYTIWKWR NYSDFKSAFG ELTIGMVGDL
     KNSRVVHSQI ELLKFFGCKF ILVAPNALKL PQKYKDLMKE NHCEFSETEN LEKVIGDFDV
     LSDTRIQQER FESEEEFKKY RTFYQIDKKM MTKAKQEMIV IAPLPRFGEL LEEVDSDPRA
     KYFEQVRNGV IVRMALIKGM IK
//
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