PYRB3_SHEHH
ID PYRB3_SHEHH Reviewed; 310 AA.
AC B0TPF3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Aspartate carbamoyltransferase 3 {ECO:0000255|HAMAP-Rule:MF_00001};
DE EC=2.1.3.2 {ECO:0000255|HAMAP-Rule:MF_00001};
DE AltName: Full=Aspartate transcarbamylase 3 {ECO:0000255|HAMAP-Rule:MF_00001};
DE Short=ATCase 3 {ECO:0000255|HAMAP-Rule:MF_00001};
GN Name=pyrB3 {ECO:0000255|HAMAP-Rule:MF_00001}; OrderedLocusNames=Shal_3052;
OS Shewanella halifaxensis (strain HAW-EB4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=458817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL Submitted (JAN-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; CP000931; ABZ77600.1; -; Genomic_DNA.
DR RefSeq; WP_012278126.1; NC_010334.1.
DR AlphaFoldDB; B0TPF3; -.
DR SMR; B0TPF3; -.
DR STRING; 458817.Shal_3052; -.
DR EnsemblBacteria; ABZ77600; ABZ77600; Shal_3052.
DR KEGG; shl:Shal_3052; -.
DR eggNOG; COG0540; Bacteria.
DR HOGENOM; CLU_043846_1_2_6; -.
DR OMA; FPTEREY; -.
DR OrthoDB; 1844275at2; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000001317; 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; Transferase.
FT CHAIN 1..310
FT /note="Aspartate carbamoyltransferase 3"
FT /id="PRO_0000334595"
SQ SEQUENCE 310 AA; 34541 MW; 201E82B83C426B82 CRC64;
MSNPIYNKHI ISISDLSRSE LELIVSTAND LKQNPRPDLL KNKVVASCFF EASTRTRLSF
ETAVQRLGGS VIGFPDSGNT SLGKKGETLA DSVQVISSYC DAFFMRHNQE GAARLASEFS
SAPVINGGDG SNQHPTQTLL DLFSIYETQG TLEKLQVAFV GDLKYGRTVH SLTQALSLFD
CEFHFIAPAA LSMPDYIIDE LKAKGCKYTL HDHLDGVLPN LDILYMTRVQ KERFDETEYQ
HLKSSFILNA NMLEGVKENL KVLHPLPRID EITTDVDSTP YAYYFQQAKN GVYARQALLA
LVLTNEFGDK
