ID   B8FB21_DESAL            Unreviewed;       357 AA.
AC   B8FB21;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=aspartate carbamoyltransferase {ECO:0000256|ARBA:ARBA00013008};
DE            EC=2.1.3.2 {ECO:0000256|ARBA:ARBA00013008};
GN   OrderedLocusNames=Dalk_2414 {ECO:0000313|EMBL:ACL04107.1};
OS   Desulfatibacillum aliphaticivorans.
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfatibacillaceae; Desulfatibacillum.
OX   NCBI_TaxID=218208 {ECO:0000313|EMBL:ACL04107.1, ECO:0000313|Proteomes:UP000000739};
RN   [1] {ECO:0000313|EMBL:ACL04107.1, ECO:0000313|Proteomes:UP000000739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK-01 {ECO:0000313|EMBL:ACL04107.1,
RC   ECO:0000313|Proteomes:UP000000739};
RX   PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA   Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA   Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT   "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT   for anaerobic alkane oxidation.";
RL   Environ. Microbiol. 14:101-113(2012).
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}.
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DR   EMBL; CP001322; ACL04107.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8FB21; -.
DR   KEGG; dal:Dalk_2414; -.
DR   eggNOG; COG0540; Bacteria.
DR   HOGENOM; CLU_043846_1_1_7; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000000739; Chromosome.
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.
PE   3: Inferred from homology;
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000739};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003634}.
FT   DOMAIN          28..177
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          189..339
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
SQ   SEQUENCE   357 AA;  41169 MW;  06CD022F11903C1F CRC64;
     MPYPYEKLTK LPAREKLTLL MRNEKLFHII FAEQFGKKTL DLLFGVATKL RKIAKSREGQ
     DFLGNLLAHK SAMLYFTQPS TRTYLSFVRA CQFLGMNYAE VRDPSISSSF KGESDIDGVR
     TFSNYFDLII MRHAEGGFAE RVAYLMNETG RPIPVISAGA GPDEHPTQAL LDLYTLNRSF
     GERAGGINGI HIAFMGDVAR GRTVRSLAKL LTRYENIHMS FVSPPELKIK EDLRKWLDRR
     GAKFQEIEDV NTIIKDIDAI YVTRIQDEYK DESIVEEEVN YEPYCLTMEQ VNLMKPTAIV
     MHPLPRRDEL DVRIDQDPRA AYWKQERNGM WIRAALVAYV FNADSLINHY YTENYSH
//