ID J7TSC1_MORMO Unreviewed; 542 AA.
AC J7TSC1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:AGG31514.1};
GN ORFNames=MU9_2469 {ECO:0000313|EMBL:AGG31514.1};
OS Morganella morganii subsp. morganii KT.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Morganella.
OX NCBI_TaxID=1124991 {ECO:0000313|EMBL:AGG31514.1, ECO:0000313|Proteomes:UP000011834};
RN [1] {ECO:0000313|EMBL:AGG31514.1, ECO:0000313|Proteomes:UP000011834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT {ECO:0000313|EMBL:AGG31514.1,
RC ECO:0000313|Proteomes:UP000011834};
RX PubMed=23282187;
RA Chen Y.T., Peng H.L., Shia W.C., Hsu F.R., Ken C.F., Tsao Y.M., Chen C.H.,
RA Liu C.E., Hsieh M.F., Chen H.C., Tang C.Y., Ku T.H.;
RT "Whole-genome sequencing and identification of Morganella morganii KT
RT pathogenicity-related genes.";
RL BMC Genomics 13:S4-S4(2012).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP004345; AGG31514.1; -; Genomic_DNA.
DR RefSeq; WP_004235317.1; NC_020418.1.
DR AlphaFoldDB; J7TSC1; -.
DR GeneID; 69678549; -.
DR KEGG; mmk:MU9_2469; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_6; -.
DR Proteomes; UP000011834; Chromosome.
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 GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 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:UP000011834};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..104
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 542 AA; 58075 MW; 4C2CD6BE72C113F0 CRC64;
MGKTIRQVTF ELLRQLNITT VFGNPGSTEE TFLKNFPADF RYIQTLHESS AVAAADGYAQ
STRNVALVNV HTSAGLSNAM SNILTAYMNR TPLIITAGNQ TRDMLLIEPW LTNIKPETLP
EPWVKWSYQP VRAEDVPAAF MRAYAMALQP PAGPVFLSIP LDDWDKPAEA DAAVVRSVSH
RISADPVRMR EFAQSVSGAK NPVLIYGSSL ARGEGWEAGI RLAEKLNIPV YSAPASERPP
FPESHPLYAG GLPFAMKPLS DKLAGHDVAL IIGAPVFRYY PYVAGDYIPP GLRLLHITDD
PQEAGRAPVG DSLLCDAVLA VEQLTELVSA RPALATAVSK QPHGMAPHPT APEAASDGLL
SASQLFRAVR SAMPEETILT EESPSNLGEL HAAWPVDKPD SFYTFASGSL GWTLPASAGI
ALGERDSGRN RPVAAIIGDG SMQYSVQGLW TAAQHQLPIL FVIPENRQYG ILKSFAVLED
TPGVPGLDIP GLDIAALATG YGCTAVRAET EAEVIAACKA ALQRKGPTVL VVPIRPSVPP
LM
//
