PYRB_MAGSA
ID PYRB_MAGSA Reviewed; 317 AA.
AC Q2W156;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 25-MAY-2022, entry version 86.
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=amb3615;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE52419.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AP007255; BAE52419.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_043745147.1; NC_007626.1.
DR AlphaFoldDB; Q2W156; -.
DR SMR; Q2W156; -.
DR STRING; 342108.amb3615; -.
DR EnsemblBacteria; BAE52419; BAE52419; amb3615.
DR KEGG; mag:amb3615; -.
DR HOGENOM; CLU_043846_2_3_5; -.
DR OMA; FPTEREY; -.
DR OrthoDB; 1844275at2; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000007058; Chromosome.
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; Reference proteome; Transferase.
FT CHAIN 1..317
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000244268"
SQ SEQUENCE 317 AA; 34902 MW; C27D8FC8A7EC1CCD CRC64;
MTDAAFPHRH LLGIQGLAPS EITSLLDLAE GYVEQNRSSD KRKNLLRGRT VINLFYENST
RTRTSFELAG KRLGADVINM QSAGSSVQKG ETLIDTAMTL NAMHLDVLVV RHPDSGAVKL
LSEKVNCAVI NGGDGSHEHP TQALLDALTI RRRKGKLSGL NVAICGDVRH SRVARSNIYL
LNAMGAHVRL IGPRTLLPSG LDRMGVEVFH DMRKGLADVD VIMMLRIQNE RMSGNFIPSI
REYFHFFGLD REKLGIAKPD AVIMHPGPMN RGVEIDSDVA DDVERSLIRS QVEMGVAVRM
ACLDMLTRDL TRSEGAV
