ID A0A1I5RT84_9BACT Unreviewed; 650 AA.
AC A0A1I5RT84;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:SFP61156.1};
GN ORFNames=SAMN04515674_104208 {ECO:0000313|EMBL:SFP61156.1};
OS Pseudarcicella hirudinis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Pseudarcicella.
OX NCBI_TaxID=1079859 {ECO:0000313|EMBL:SFP61156.1, ECO:0000313|Proteomes:UP000199306};
RN [1] {ECO:0000313|EMBL:SFP61156.1, ECO:0000313|Proteomes:UP000199306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E92,LMG 26720,CCM 7988 {ECO:0000313|Proteomes:UP000199306};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FOXH01000004; SFP61156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5RT84; -.
DR STRING; 1079859.SAMN04515674_104208; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000199306; 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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000199306};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 19..123
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 207..343
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 444..581
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 650 AA; 71505 MW; 3452B9B222DF30D1 CRC64;
METTVNHPQR PGIPTKRWTR DYVFDVLKDL GIHYIFGVPG TNEIPIIDGT SYPENKVRYI
ECLHENIAIG AAMGSARMTG KPGVLVVHVT PGIAHTIGNL FNACRSQTPL VILCCQQQNE
LVTQEPLLAS NLVDLAKQYT KWAHEVRTPA EIPLVLQRAF KEAMAPPNGP VFISIPWEFT
MVRIPDDAHM KGITRISSHF TGDPESIRQT ALLLAQAKNP IIVAGDAVGY ADAWSEVQEL
AQLIGAPVSL QTFSSVANYP NNDIHWQGEL PGVQASIRQV FDGHDVAFLV GFGAQAQLAV
FKYSDGPLIP DHVKQIYLTN NTWDIGKNSY GESAVLGDIK ATLPLINAIV KSHGSEGADA
RNKHLEALDL QRKKQWAVYK EKALHQKEIW AVLIADALRE AIEEKGLANK FVYVHEAVSD
GAPFQYLLPF GTHSSKPISY YCVAGGSLGW SMPASLGIKL EPQGSQGIET TLVVNAVGDG
SSLFYPQTYW TAAHQNLAVL YIITNNREYH TLQVGLQQVI AAYGSAPGYE WQPATTDPEY
LRINRPKFDF VSLAKAFGGE NGEVVKDPAS VKEAVFRGVQ HVITNKTSYI LDMRTAQDTP
PPATKEEAED QLYKKYLEQP SLDIFHEQTH VAGARKSAEN NIPANVPSLF
//
