ID Q9KUH1_VIBCH Unreviewed; 597 AA.
AC Q9KUH1;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 119.
DE SubName: Full=Oxaloacetate decarboxylase, alpha subunit {ECO:0000313|EMBL:AAF93718.1};
GN OrderedLocusNames=VC_0550 {ECO:0000313|EMBL:AAF93718.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF93718.1, ECO:0000313|Proteomes:UP000000584};
RN [1] {ECO:0000313|EMBL:AAF93718.1, ECO:0000313|Proteomes:UP000000584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961
RC {ECO:0000313|Proteomes:UP000000584};
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D.,
RA Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.,
RA Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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DR EMBL; AE003852; AAF93718.1; -; Genomic_DNA.
DR PIR; G82308; G82308.
DR RefSeq; NP_230201.1; NC_002505.1.
DR AlphaFoldDB; Q9KUH1; -.
DR SMR; Q9KUH1; -.
DR STRING; 243277.VC_0550; -.
DR DNASU; 2615227; -.
DR EnsemblBacteria; AAF93718; AAF93718; VC_0550.
DR KEGG; vch:VC_0550; -.
DR PATRIC; fig|243277.26.peg.526; -.
DR eggNOG; COG0511; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR HOGENOM; CLU_000395_4_3_6; -.
DR OMA; GYHALEM; -.
DR BRENDA; 4.1.1.112; 6626.
DR Proteomes; UP000000584; 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:UP000000584}.
FT DOMAIN 7..267
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 518..597
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 597 AA; 64795 MW; 033BF5F2209F5468 CRC64;
MSMSKPLAIT DVVLRDAHQS LFATRMRIED MLPIAAELDK IGYWSLETWG GATFDACIRF
LGEDPWERLR ALKKAMPNTP MQMLLRGQNL LGYRHYADDV VEKFVERAHV NGMDVFRIFD
AMNDVRNFEK AVKATIGVGA HAQGTLSYTT SPVHNTQTWV DLAKRLEDLG CHSLCIKDMS
GLLKPYEAEE LITRIKQSCA VPLALHCHAT TGLSTATAVK AVEAGIDILD TAISSMSQTY
GHTPTETVVA MLQDTPRDTQ LKLEQLEPIA AYFREVRKKY AKFEGQLKGV DSRILIAQVP
GGMLTNMESQ LKEQGAAHRI DEVLEEIPRV RQDLGFIPLV TPTSQIVGTQ AVINVLTGER
YKSITKETAG VLKGEYGATP ASVNAELQAR VLEGGQAITC RPADLLQDEL DHLTKELLEK
AQVEKITLAD AKVDDVLTYA LFPQVGLKFL KNRHNPEAFE PAPGKEPAPV ATAPASTKPA
AGIESYSVKV DGVVYDVEVG SQGQLTSVVP AGQKAAPKLA VATPTQGAEA VAAPLAGTIF
KIQVEQGDEV AEGDVLIVLE AMKMETEIRA ARSGVIQELH VKEGDSVRVG ASLLSLA
//