ID   PYRB_HELPS              Reviewed;         307 AA.
AC   B2USJ6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Aspartate carbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_00001};
DE            EC=2.1.3.2 {ECO:0000255|HAMAP-Rule:MF_00001};
DE   AltName: Full=Aspartate transcarbamylase {ECO:0000255|HAMAP-Rule:MF_00001};
DE            Short=ATCase {ECO:0000255|HAMAP-Rule:MF_00001};
GN   Name=pyrB {ECO:0000255|HAMAP-Rule:MF_00001}; OrderedLocusNames=HPSH_01890;
OS   Helicobacter pylori (strain Shi470).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=512562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shi470;
RA   Kersulyte D., Kalia A., Gilman R.H., Berg D.E.;
RT   "Genome sequence of Helicobacter pylori from the remote Amazon: traces of
RT   Asian ancestry of the first Americans.";
RL   Submitted (MAY-2008) 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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00001};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000255|HAMAP-
CC       Rule:MF_00001}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000255|HAMAP-Rule:MF_00001}.
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DR   EMBL; CP001072; ACD47828.1; -; Genomic_DNA.
DR   RefSeq; WP_001124595.1; NC_010698.2.
DR   AlphaFoldDB; B2USJ6; -.
DR   SMR; B2USJ6; -.
DR   KEGG; hps:HPSH_01890; -.
DR   HOGENOM; CLU_043846_2_0_7; -.
DR   OMA; FPTEREY; -.
DR   UniPathway; UPA00070; UER00116.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-UniRule.
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:cellular amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1370; -; 2.
DR   HAMAP; MF_00001; Asp_carb_tr; 1.
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   PANTHER; PTHR11405:SF16; PTHR11405:SF16; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Pyrimidine biosynthesis; Transferase.
FT   CHAIN           1..307
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_1000088770"
SQ   SEQUENCE   307 AA;  34140 MW;  5E0B8BE7C12BFA1D CRC64;
     MPKKCRHLLQ TSDLSLDEIK LLLKKASVYA NDFNAVSLET KEKMQNKIIV ALFFENSTRT
     VSSFEIASLR LGAKIVKLNM QTSSASKGET LTDTFKNIYA MQPDAIITRH AFSSAPFKLA
     EFSQCPLINA GSGVSAHPTQ ALLDLLTLYQ HFGSLENLKG KKIAFIGDVK NSRVANSNIK
     LLQRLGLEIM LCAPSSMLPS VSLKTTHNIE EAIEFADILM SLRTQTERHN APIFASLKDY
     GNAYCITQKR LEAHAKNKEI IILHPGPVHR DIDIESAVLE DKRSKVLEQV KNGVAMRMAV
     LEFLLLD