ID A0A0R3DZZ0_9BRAD Unreviewed; 540 AA.
AC A0A0R3DZZ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:KRQ15527.1};
DE EC=4.1.1.7 {ECO:0000313|EMBL:KRQ15527.1};
GN ORFNames=AOQ71_09050 {ECO:0000313|EMBL:KRQ15527.1};
OS Bradyrhizobium manausense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=989370 {ECO:0000313|EMBL:KRQ15527.1, ECO:0000313|Proteomes:UP000051936};
RN [1] {ECO:0000313|EMBL:KRQ15527.1, ECO:0000313|Proteomes:UP000051936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR3351 {ECO:0000313|EMBL:KRQ15527.1,
RC ECO:0000313|Proteomes:UP000051936};
RA De Araujo J.L., Zilli J.E.;
RT "Draft Genome Sequence of Bradyrhizobium manausense Strain BR 3351T, a
RT Novel Symbiotic Nitrogen-Fixing Alphaproteobacterium Isolated from
RT Brazilian Amazon Rain Forest.";
RL Submitted (SEP-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:KRQ15527.1}.
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DR EMBL; LJYG01000042; KRQ15527.1; -; Genomic_DNA.
DR RefSeq; WP_057744685.1; NZ_LJYG01000042.1.
DR AlphaFoldDB; A0A0R3DZZ0; -.
DR STRING; 989370.AOQ71_09050; -.
DR OrthoDB; 9773408at2; -.
DR Proteomes; UP000051936; Unassembled WGS sequence.
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 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:KRQ15527.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 13..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..331
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 384..526
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 540 AA; 57141 MW; 9AD5F2908D683CFB CRC64;
MAKNGKTGSK SVTVKQATLD LLRAFGITKV FGNPGSTELP FLSDWPDDID YVLALQEASA
VGMADGYAQA TRNAGFVNLH SAAGVGNALG NIYTAHRNQT PLVITAGQQA RSILPLQAFL
YAERASEFPR PYVKYSVEPA RPEDVPAAIA RAYYTAMQPP CGPTFVSIPI DDWTHATPPV
EARRVSREIG PELDAMKALA AALAIAKHPA LVVGPGVDRA GAVDLMVRVA EKAKASVWVS
PFSARCSFPE RHPQFAGFLH ASPAQLSDAL REHDLVVVIG APVFTFHVEG HAAIFDGGAT
IFQITDDPDA AAVTPSGTSI IATMKPALTA LLDLLPESQR AAPKGRTLPP APQAADPLPV
EFLLHALSQA MPEGASLVEE VPSHRPAMQK FLPMPGQDSF YTMSSGGLGY SLPAAVGMAL
GKPKQRTVCL IGDGSAMYSI QALWTAAQRK LPLTIVVINN SGYGAMRSFS QVMQVRNVPG
LELPGIDFVR LAEGMGCHAV RVSKAAELGA ALKRGMTFEG TSLVEVVVDS AVPVLYGQKH
//
