MDLC_PSEAE
ID MDLC_PSEAE Reviewed; 528 AA.
AC Q9HUR2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Benzoylformate decarboxylase;
DE Short=BFD;
DE Short=BFDC;
DE EC=4.1.1.7;
GN Name=mdlC; OrderedLocusNames=PA4901;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + phenylglyoxylate = benzaldehyde + CO2;
CC Xref=Rhea:RHEA:23368, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17169, ChEBI:CHEBI:36656; EC=4.1.1.7;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per dimer. {ECO:0000250};
CC -!- PATHWAY: Aromatic compound metabolism; (R)-mandelate degradation;
CC benzoate from (R)-mandelate: step 3/4.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; AE004091; AAG08286.1; -; Genomic_DNA.
DR PIR; C83033; C83033.
DR RefSeq; NP_253588.1; NC_002516.2.
DR RefSeq; WP_003099962.1; NC_002516.2.
DR AlphaFoldDB; Q9HUR2; -.
DR SMR; Q9HUR2; -.
DR STRING; 287.DR97_2252; -.
DR PaxDb; Q9HUR2; -.
DR EnsemblBacteria; AAG08286; AAG08286; PA4901.
DR GeneID; 882177; -.
DR KEGG; pae:PA4901; -.
DR PATRIC; fig|208964.12.peg.5134; -.
DR PseudoCAP; PA4901; -.
DR HOGENOM; CLU_013748_3_1_6; -.
DR InParanoid; Q9HUR2; -.
DR OMA; DFRHEEP; -.
DR PhylomeDB; Q9HUR2; -.
DR BioCyc; PAER208964:G1FZ6-5015-MON; -.
DR UniPathway; UPA00873; UER00854.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR GO; GO:0050695; F:benzoylformate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0019596; P:mandelate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR18968; PTHR18968; 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; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Calcium; Decarboxylase; Lyase; Magnesium;
KW Mandelate pathway; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate.
FT CHAIN 1..528
FT /note="Benzoylformate decarboxylase"
FT /id="PRO_0000287823"
FT REGION 377..460
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
SQ SEQUENCE 528 AA; 55673 MW; 83045771D88435EC CRC64;
MKTVHSASYE ILRRHGLTTV FGNPGSNELP FLKDFPEDFR YILGLHEGAV VGMADGFALA
SGRPAFVNLH AAAGTGNGMG ALTNAWYSHS PLVITAGQQV RSMIGVEAML ANVDAGQLPK
PLVKWSHEPA CAQDVPRALS QAIQTASLPP RAPVYLSIPY DDWAQPAPAG VEHLAARQVS
GAALPAPALL AELGERLSRS RNPVLVLGPD VDGANANGLA VELAEKLRMP AWVAPSASRC
PFPTRHACFR GVLPAAIAGI SRLLDGHDLI LVVGAPVFRY HQFAPGDYLP AGAELVQVTC
DPGEAARAPM GDALVGDIAL TLEALLEQVR PSARPLPEAL PRPPALAEEG GPLRPETVFD
VIDALAPRDA IFVKESTSTV TAFWQRVEMR EPGSYFFPAA GGLGFGLPAA VGAQLAQPRR
QVIGIIGDGS ANYGITALWS AAQYRVPAVF IILKNGTYGA LRWFAGVLEV PDAPGLDVPG
LDFCAIARGY GVEALHAATR EELEGALKHA LAADRPVLIE VPTQTIEP
