ID Q7VFJ0_HELHP Unreviewed; 599 AA.
AC Q7VFJ0;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 24-JAN-2024, entry version 99.
DE SubName: Full=Oxaloacetate decarboxylase {ECO:0000313|EMBL:AAP78283.1};
DE EC=4.1.1.3 {ECO:0000313|EMBL:AAP78283.1};
GN Name=pycB {ECO:0000313|EMBL:AAP78283.1};
GN OrderedLocusNames=HH_1686 {ECO:0000313|EMBL:AAP78283.1};
OS Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=235279 {ECO:0000313|EMBL:AAP78283.1, ECO:0000313|Proteomes:UP000002495};
RN [1] {ECO:0000313|EMBL:AAP78283.1, ECO:0000313|Proteomes:UP000002495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51449 / 3B1 {ECO:0000313|Proteomes:UP000002495};
RX PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA Shen Z., Weber J., Frosch M., Fox J.G.;
RT "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT hepaticus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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DR EMBL; AE017125; AAP78283.1; -; Genomic_DNA.
DR RefSeq; WP_011116525.1; NC_004917.1.
DR AlphaFoldDB; Q7VFJ0; -.
DR STRING; 235279.HH_1686; -.
DR GeneID; 82136205; -.
DR KEGG; hhe:HH_1686; -.
DR eggNOG; COG0511; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR HOGENOM; CLU_000395_4_2_7; -.
DR OMA; EAGMISQ; -.
DR OrthoDB; 9769961at2; -.
DR Proteomes; UP000002495; Chromosome.
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 Lyase {ECO:0000313|EMBL:AAP78283.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002495}.
FT DOMAIN 2..262
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 524..599
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 599 AA; 66306 MW; F34D3C4CD14CD3C0 CRC64;
MIKITENSLR DGHQSLLATR MRTQDLLEAA KIFDSIGFHS VEVWGGATYD TCLRYLKEDP
FERLNEFKKV FVKTPLQMLL RGQNLIGYRH YADDVVEEFV RLSSEAGMDI FRIFDAFNDA
RNLRVSIESV KKYGKHAQGA ICYTTSPVHT ISSFVDYAKE LVEMGCDSIA IKDMAGLLTP
FTAYDLVKAL KEELGVYLCL HTHSTAGFAF GAHLKAVEAG VDVLDLANSA LSEGTSHPCT
QSMVATLRGT KWDTKLDIAS MEIAAEILRK NRRKYKKFES QYNQIDTRVL VNQIPGGMIS
NMANQLKEQN ALDRMEEVMQ EIPNVRADFG YVPLVTPSSQ IVGTQAVLNV LMGERYKTIT
TETRNVIKGL YGRTPAPLNE MLVKKVLSEG EDIVRVRPAD LLSPELKKAK EESAGFAKSA
QDVISYAMFG TIAQTFLQER NANALNPEPL ESYEEKCDDK LPKEFEIVVN GEHYAIKIEG
SGEKTDEVRP FFIRVDGELK EVFVESISTP LGGKVIKEQK AGALPQATAP GHAKSPMPGT
LTKLKVKVGD KVKQGDTLAI VEAMKMENEV LSPIDGVVKE IYATQGAQIG SDVAIMLLG
//