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Database: UniProt
Entry: A0A0Q6PRZ6_9MICO
LinkDB: A0A0Q6PRZ6_9MICO
Original site: A0A0Q6PRZ6_9MICO 
ID   A0A0Q6PRZ6_9MICO        Unreviewed;       534 AA.
AC   A0A0Q6PRZ6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:KQV06319.1};
GN   ORFNames=ASC63_02320 {ECO:0000313|EMBL:KQV06319.1};
OS   Leifsonia sp. Root112D2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV06319.1, ECO:0000313|Proteomes:UP000051914};
RN   [1] {ECO:0000313|EMBL:KQV06319.1, ECO:0000313|Proteomes:UP000051914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root112D2 {ECO:0000313|EMBL:KQV06319.1,
RC   ECO:0000313|Proteomes:UP000051914};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV06319.1, ECO:0000313|Proteomes:UP000051914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root112D2 {ECO:0000313|EMBL:KQV06319.1,
RC   ECO:0000313|Proteomes:UP000051914};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQV06319.1}.
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DR   EMBL; LMCU01000001; KQV06319.1; -; Genomic_DNA.
DR   RefSeq; WP_055809395.1; NZ_LMCU01000001.1.
DR   AlphaFoldDB; A0A0Q6PRZ6; -.
DR   STRING; 1736426.ASC63_02320; -.
DR   OrthoDB; 2443624at2; -.
DR   Proteomes; UP000051914; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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: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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051914};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          3..116
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          191..325
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          390..526
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   534 AA;  55346 MW;  1D79F80AED81A405 CRC64;
     MATVRDVTYD ILRQNGLTTI FGNPGSNELP FLDRMPADFR YILGLQEAVV AGMADGYSLV
     TGEPVFVNLH SAAGTGNAMG AIANAWYSHS PLVISAGQQA RSLVGPEAML SNVDATQLPR
     PLVKVSLEPS LATDVPRAIS QAIHTATAAP RGPVYVSIPW DDWAEDAGES SAFLASRVVV
     TAGAPSAQQL ADIVSRVEAS ANPVLILGAD VDAAGAGALA VQLAERQRMP VWVAPSASRC
     PFPTRHPCFR GVLPSSIAGL SGRLAGHDLI LVIGAPVFRY HQFQPGRYLP SGAELIQITS
     DAGEAARAPM GDALIADVGF ALQALVSSVS VSSREMPLAR ALPAPAAVSA SASADGALSL
     EALFDVVNEV APEDAIYVRE ATTTNEAFWD RIEMKHPGSY LFPAAGGLGF GMPATVGAQL
     ASAHRRVIGI IGDGSANYGI TALWTAAQYR IPAIFLIVKN GTYGGLRSFA KQLGADDIPG
     MDLPGLDFCA LASGYGVRSS VADSAAALRE SLAAALAADT PTLIEIPIRS TPAS
//
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