ID A0A102D9M7_9SPHN Unreviewed; 530 AA.
AC A0A102D9M7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:KUR77486.1};
DE EC=4.1.1.7 {ECO:0000313|EMBL:KUR77486.1};
GN ORFNames=AQZ50_09795 {ECO:0000313|EMBL:KUR77486.1};
OS Novosphingobium sp. Fuku2-ISO-50.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1739114 {ECO:0000313|EMBL:KUR77486.1, ECO:0000313|Proteomes:UP000056630};
RN [1] {ECO:0000313|EMBL:KUR77486.1, ECO:0000313|Proteomes:UP000056630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fuku2-ISO-50 {ECO:0000313|EMBL:KUR77486.1,
RC ECO:0000313|Proteomes:UP000056630};
RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA Glaeser S.;
RT "Draft genome sequence of Novosphingobium sp. Fuku2-ISO-50 (=DSM 27930), a
RT Novosphingobium acidiphilum related species isolated from a surface water
RT sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUR77486.1}.
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DR EMBL; LLZR01000013; KUR77486.1; -; Genomic_DNA.
DR RefSeq; WP_067746015.1; NZ_KQ954290.1.
DR AlphaFoldDB; A0A102D9M7; -.
DR STRING; 1739114.AQZ50_09795; -.
DR OrthoDB; 9773408at2; -.
DR Proteomes; UP000056630; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF133; BENZOYLFORMATE DECARBOXYLASE; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KUR77486.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000056630};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..294
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..526
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 530 AA; 55270 MW; A308C96D3A6F15FA CRC64;
MPESPAIGAT AACPSTVRDV TIDLLRAAGM TTIFGNPGST ELPMFRDFPD DFRYILGLQE
SVAVAMADGF ATATRKAALI NLHSSAGVGH ALGAVFTAFR NQTPLVITAG QQARSILPYE
PFLFAERPSE FPRPFVKWAV EPARAQDVPA AIARAYAVAM EPPCGPTFVS VPVDDWDQPC
APLTLRPISA TRHPDPAALA QCAQSLARAR RPAIAVAAGV ARDCAWDLVV ALAERHGASV
YVAPMASRAG FPEDHPLFAG FLAASREAIV ASLAPHDVVL ALGGPMNLYH VEGHGPHLPD
GCEAWLIGDN HTHAAWAPQG RAIVASCDVA IAGLLAGPDP VARAWPAPRI VAPVAGDVMT
DALVVSRLAA LRAPGSILVE EAPSTRGPMH DHLPILRPDT FYTTASGGLG FALPAAVGIA
LARPGEKVIA LLGDGSSMYA IQGLFSAAAL GLPISFIIIR NGRYEALHSF GRHFGLQQPV
GTELPVLDFC ALAAGHGVPA RRADDAATLE EALCWSLAAD GPTLVEAVVA
//