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
//