ID Q87LR7_VIBPA Unreviewed; 595 AA.
AC Q87LR7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 95.
DE SubName: Full=Oxaloacetate decarboxylase, alpha subunit {ECO:0000313|EMBL:BAC60807.1};
GN OrderedLocusNames=VP2544 {ECO:0000313|EMBL:BAC60807.1};
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC60807.1, ECO:0000313|Proteomes:UP000002493};
RN [1] {ECO:0000313|EMBL:BAC60807.1, ECO:0000313|Proteomes:UP000002493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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DR EMBL; BA000031; BAC60807.1; -; Genomic_DNA.
DR RefSeq; NP_798923.1; NC_004603.1.
DR RefSeq; WP_005480900.1; NC_004603.1.
DR AlphaFoldDB; Q87LR7; -.
DR GeneID; 1190059; -.
DR KEGG; vpa:VP2544; -.
DR PATRIC; fig|223926.6.peg.2441; -.
DR eggNOG; COG0511; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR HOGENOM; CLU_000395_4_3_6; -.
DR OMA; GYHALEM; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR005776; OadA.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01108; oadA; 1.
DR PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Reference proteome {ECO:0000313|Proteomes:UP000002493}.
FT DOMAIN 5..265
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 519..595
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 595 AA; 64276 MW; 0DCE581EFBA22F0A CRC64;
MSKPLAITDV VLRDAHQSLF ATRMRIEDML PIAAELDKIG YWSLETWGGA TFDSCIRFLG
EDPWERLREL KKAMPNTPMQ MLLRGQNLLG YRHYADDVVE KFVERAHANG MDVFRIFDAM
NDVRNFQKAV KSAVDVGAHA QGTLSYTTSP VHNTDTWVDL AKRLEDLGCH SLCIKDMSGL
LKPYEAQELI TRIKASCDVP LALHCHATTG LSTATAIKAV EAGIDILDTA ISSMSCTYGH
TPTETVVAML QGTERDTNLK LDQLEPIAAY FREVRKKYAK WEGQLKGVDS RILIAQVPGG
MLTNMEGQLK EQGAADRIDE VLEEIPRVRE DLGFIPLVTP TSQIVGTQAV INVLTGERYK
SITKETAGVL KGEYGAAPAA VNAELQAKVL EGKEPITCRP ADLLESEMEA LTVDLMEKAQ
SEGIKLASER VDDVLTYALF PQVGLKFLKN RGNPDAFEPA PTLESAKPVA APAAPVASGS
VETYSVRVDG QVYEVEVGPK GQLTSVTPSS ASVPVAAPVA PVTTNAESVP APLAGNIFKV
NVQPGAEVAE GDVLLILEAM KMETEVRAAR GGIVQELNVK EGDAVTVGAP LLSLA
//