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Database: UniProt
Entry: A0A1W6Z1G7_9BORD
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ID   A0A1W6Z1G7_9BORD        Unreviewed;       430 AA.
AC   A0A1W6Z1G7;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=aspartate carbamoyltransferase {ECO:0000256|ARBA:ARBA00013008};
DE            EC=2.1.3.2 {ECO:0000256|ARBA:ARBA00013008};
GN   ORFNames=CAL13_13760 {ECO:0000313|EMBL:ARP87156.1};
OS   Bordetella genomosp. 9.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1416803 {ECO:0000313|EMBL:ARP87156.1, ECO:0000313|Proteomes:UP000194139};
RN   [1] {ECO:0000313|EMBL:ARP87156.1, ECO:0000313|Proteomes:UP000194139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU17164 {ECO:0000313|EMBL:ARP87156.1,
RC   ECO:0000313|Proteomes:UP000194139};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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. ATCase family. {ECO:0000256|ARBA:ARBA00008896}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000256|ARBA:ARBA00007805}.
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DR   EMBL; CP021109; ARP87156.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6Z1G7; -.
DR   OrthoDB; 9774690at2; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000194139; 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:0004585; F:ornithine 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   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   Reference proteome {ECO:0000313|Proteomes:UP000194139};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003634}.
FT   DOMAIN          90..229
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          242..396
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
SQ   SEQUENCE   430 AA;  47785 MW;  ED9F4F845780B32F CRC64;
     MSISQQAFLR DAMRRLNLTR DVFAARIGVK RRALDTWLLP EGSQEYRAMP EVVERFVTEI
     VQNGVLREKY TQSAQNGPLR DRIAVEGKHQ LLSVDQFSRE SVEDLFRIAD MMQPIARRQK
     VSRVLEGAVL GNLFFEASTR TRVSFGAAFC RLGGSVCDTT GFTFSSMAKG ESIYDTSRVM
     SGYVDAMVIR HPEQGSVAEF ARATNIPVVN GGDGPGEHPS QALLDLYTIL TEFSRLGKLL
     DGAHIAMVGD LKYGRTVHSL IKLLSLYRGV KFTLIAPPGL EMPSYIIEQA ARHDNVIEQK
     QSLAEGLAGA DVIYATRVQK ERFADEAQEG YTPDFQINRA IIDTYCGPDT IVMHPLPRDS
     RPGANDLSVD LNHDPRLAIF RQTDNGIPIR MAIFAVLLGV EGLVQHSMRD VTWRHPSHIG
     PDDSAFHGLD
//
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