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Database: UniProt
Entry: A0A102D9M7_9SPHN
LinkDB: A0A102D9M7_9SPHN
Original site: A0A102D9M7_9SPHN 
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
//
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