ID V8CEY2_9HELI Unreviewed; 305 AA.
AC V8CEY2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Aspartate carbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_00001};
DE EC=2.1.3.2 {ECO:0000256|HAMAP-Rule:MF_00001};
DE AltName: Full=Aspartate transcarbamylase {ECO:0000256|HAMAP-Rule:MF_00001};
DE Short=ATCase {ECO:0000256|HAMAP-Rule:MF_00001};
GN Name=pyrB {ECO:0000256|HAMAP-Rule:MF_00001};
GN ORFNames=HMPREF2087_01758 {ECO:0000313|EMBL:ETD25924.1};
OS Helicobacter canis NCTC 12740.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1357399 {ECO:0000313|EMBL:ETD25924.1, ECO:0000313|Proteomes:UP000018688};
RN [1] {ECO:0000313|EMBL:ETD25924.1, ECO:0000313|Proteomes:UP000018688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 12740 {ECO:0000313|EMBL:ETD25924.1,
RC ECO:0000313|Proteomes:UP000018688};
RG The Broad Institute Genomics Platform;
RA Earl A., Fox J.G., Shen Z., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Abouelleil A., Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Helicobacter canis NCTC 12740.";
RL Submitted (OCT-2013) 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, ECO:0000256|HAMAP-
CC Rule:MF_00001};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00004852, ECO:0000256|HAMAP-Rule:MF_00001}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000256|HAMAP-Rule:MF_00001}.
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:ETD25924.1}.
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DR EMBL; AZJJ01000007; ETD25924.1; -; Genomic_DNA.
DR RefSeq; WP_023930816.1; NZ_KI669458.1.
DR AlphaFoldDB; V8CEY2; -.
DR STRING; 1357399.HMPREF2087_01758; -.
DR PATRIC; fig|1357399.3.peg.1847; -.
DR eggNOG; COG0540; Bacteria.
DR HOGENOM; CLU_043846_2_0_7; -.
DR OrthoDB; 9774690at2; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000018688; Unassembled WGS sequence.
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:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 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 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, ECO:0000256|HAMAP-
KW Rule:MF_00001}; Reference proteome {ECO:0000313|Proteomes:UP000018688};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00001}.
FT DOMAIN 2..150
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 158..298
FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00185"
SQ SEQUENCE 305 AA; 33599 MW; D699AA13E7AE5C7D CRC64;
MRHLIETSDL STDEIERILH KATQFLPMLD STTLDSSKRP AQSLAHTNII TIFFENSTRT
LSSFECAVKN LGGSITRLDV SRSSTSKGET ISDTAANLNA MSPHAIIIRH QSSGAPVHLT
KSVSCPIING GDGAHAHPTQ ALLDLLTLRQ CLGQNLAGKR IGIIGDIKTS RVANSNIELL
SRYGAELVLI APPHFLPPHS KLAYTHDITE VIDSLHAIIS LRTQTERHSK QNYGSLRDYA
NQFCLTKQLI GDRDIVIMHP GPVHHNIDIE DELLKDSRCK VLQQVRNGVA VRMAVLEFFI
LETKA
//