ID A4YN55_BRASO Unreviewed; 560 AA.
AC A4YN55;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:CAL75331.1};
DE EC=4.1.1.7 {ECO:0000313|EMBL:CAL75331.1};
GN Name=mdlC {ECO:0000313|EMBL:CAL75331.1};
GN OrderedLocusNames=BRADO1439 {ECO:0000313|EMBL:CAL75331.1};
OS Bradyrhizobium sp. (strain ORS 278).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=114615 {ECO:0000313|EMBL:CAL75331.1, ECO:0000313|Proteomes:UP000001994};
RN [1] {ECO:0000313|EMBL:CAL75331.1, ECO:0000313|Proteomes:UP000001994}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ORS 278 {ECO:0000313|Proteomes:UP000001994};
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CU234118; CAL75331.1; -; Genomic_DNA.
DR AlphaFoldDB; A4YN55; -.
DR STRING; 114615.BRADO1439; -.
DR KEGG; bra:BRADO1439; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_5; -.
DR Proteomes; UP000001994; Chromosome.
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:CAL75331.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001994};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 33..135
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 216..349
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 404..546
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 560 AA; 59618 MW; 62EB303E097DAF6D CRC64;
MPGTLDCFVA SLLAMTAIRG TPLAKKTTTK PVTVKQATFD LLRAFGIKKV FGNPGSTELP
FLSDWPDDID YVLGLQEASV VGMADGYAQA TRNAGFVNLH SAAGVGNALG NIYTAHRNQT
PLVITAGQQA RSILPLQAFL YAERPSEFPR PYVKYSVEPA RPEDVPGAIA RAYYTAMQPP
CGPTFVSIPI DDWMHPAQPV AARKVSRELG PDRAAIEELV AALGAAKNPA LVVGPGIDRA
ACVDLMVQVA EKAKAGVWVS PFSARCSFPE RHPQFQGFLH ASPGQLSEAL KPYDIVVVIG
APVFTFHVEG HAAIFDGATT LYQITDDAEG ASVPPIGTSI VATMRPALSL LRELLPESQR
AAPKGRVMPE PPDASDPIPV DYLLHTLSQA LPPGAAIVEE IPSHRPVMYK YMPMPGADSF
YTMASGGLGY SLPASVGMAL GRPNDRIVCL IGDGSAMYSL QALWTAAQRK LRLTIVVINN
SGYGAMRSFS QVMQVRNVPG LELPGLDFVK LAEGLGCDAV RVSRSADLPA ALARGLAHDG
TSLVEVMVDS AVPLLYAQKR
//
