ID Q7NTF5_CHRVO Unreviewed; 638 AA.
AC Q7NTF5;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:AAQ60769.1};
DE EC=4.1.1.7 {ECO:0000313|EMBL:AAQ60769.1};
GN Name=mdlC {ECO:0000313|EMBL:AAQ60769.1};
GN OrderedLocusNames=CV_3101 {ECO:0000313|EMBL:AAQ60769.1};
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365 {ECO:0000313|EMBL:AAQ60769.1, ECO:0000313|Proteomes:UP000001424};
RN [1] {ECO:0000313|EMBL:AAQ60769.1, ECO:0000313|Proteomes:UP000001424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 /
RC NCTC 9757 {ECO:0000313|Proteomes:UP000001424};
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Almeida F.C., de Almeida L.G.P.,
RA de Almeida R., Goncalves J.A.A., Andrade E.M., Antonio R.V., Araripe J.,
RA de Araujo M.F.F., Filho S.A., Azevedo V., Batista A.J., Bataus L.A.M.,
RA Batista J.S., Belo A., vander Berg C., Blamey J., Bogo M., Bonato S.,
RA Bordignon J., Brito C.A., Brocchi M., Burity H.A., Camargo A.A.,
RA Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B.,
RA Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Pasa T.B.C., Duran N.,
RA Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S.,
RA Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A.,
RA Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Guimaraes C.T., Hanna E.S., Hungria M.,
RA Jardim S.N., Laurino J., Leoi L.C.T., Fassarella L., Lima A.,
RA Loureiro M.F., Lyra M.C.P., Macedo M., Madeira H.M.F., Manfio G.P.,
RA Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B.,
RA Meissner R.D.V., Menck C.F.M., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.J.D., Perreira J.O., Perreira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Neto C.E.R., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., dos Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; AE016825; AAQ60769.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7NTF5; -.
DR STRING; 243365.CV_3101; -.
DR KEGG; cvi:CV_3101; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_3_4; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000001424; Chromosome.
DR GO; GO:0050695; F:benzoylformate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02002; TPP_BFDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AAQ60769.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001424};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 13..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..337
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 438..576
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 638 AA; 70737 MW; A809FF268D751430 CRC64;
MSVDEAGGQK RWARDYVFDI LSQLGIHRIF GVPGTNEIPI IDGTSYPENQ VEYIECLHEN
IAIGAAMGSA RMTGKPGVLV VHVTPGIAHA IGNLFNAWRS QAPLVVLCCQ QQNELVTQEP
LLASNLVDLA RQYTKWAHEV RTEQEFPMVL QRAFKEAMAP PNGPVFVAIP WEFTMRRIGD
DDRIKGVTRI SPHFTADRRA IDQAAQLLRE ARNPIIVTGD AAGYAEAWPE LQRMAELLGA
PVLQQTFSSL ANFPNNDYHW QGELPGSQSG VQQVFAGHDV AFLCGFSNQA QITVYKYSDG
PLIPPDVTQV YLSNHTWDIG KNYYGEAALF GDLKATLPLI NQLIGDQPSP AAAARNAKLK
EMAAQRKVAW DAYLREAMHQ NEIWAVVIAD ALRKEIGERK LEKQFVYVHE AVSDPAPFQY
LLPFTDEAAA PISYYCVGGG SLGWSMPATL GIKLEPSGCQ DINTRFVVAA TGDGSSLFYP
QTWWTAQHRQ LGVLYIIITN NHEYHTLQMG LTQVEAMYGE APGYEWTART QDPEYLRIHR
PKPDFVTLAK AFGGMEGEIV RHPEDVRAAV RRGIDHALSG HAYVLDMHTV GLDQPPPTPE
DANARYDKQP RLDCFHFGAD AQQRNDGAGL PGNVPVIF
//
