ID Q122C9_POLSJ Unreviewed; 731 AA.
AC Q122C9;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Thiamine pyrophosphate enzyme-like TPP-binding protein {ECO:0000313|EMBL:ABE46613.1};
DE EC=1.2.7.8 {ECO:0000313|EMBL:ABE46613.1};
GN OrderedLocusNames=Bpro_4734 {ECO:0000313|EMBL:ABE46613.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE46613.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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DR EMBL; CP000316; ABE46613.1; -; Genomic_DNA.
DR RefSeq; WP_011485598.1; NC_007948.1.
DR AlphaFoldDB; Q122C9; -.
DR STRING; 296591.Bpro_4734; -.
DR KEGG; pol:Bpro_4734; -.
DR eggNOG; COG4231; Bacteria.
DR HOGENOM; CLU_017727_0_0_4; -.
DR OrthoDB; 9804603at2; -.
DR Proteomes; UP000001983; Chromosome.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02008; TPP_IOR_alpha; 1.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR045025; HACL1-like.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR PANTHER; PTHR43710:SF5; INDOLEPYRUVATE FERREDOXIN OXIDOREDUCTASE ALPHA SUBUNIT; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:ABE46613.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983}.
FT DOMAIN 627..658
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 532..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 731 AA; 79182 MW; DD567B0007327754 CRC64;
MAERSFTNEV QKLRLGDGDE FRGEGILAVT KALLQSGVSY VAGYQGAPIS HLMDVLTDAN
DILQELGVRF EHSASEATAT ATLAASVNYP LRGAVTFKST VGTNVASDAL ANLASGGVTG
GAMLIVGEDY GEGSSIMQER SHAFAMKSQV WLIDPRPNLE SIVRAVEMGF ELSEASRTPV
MLELRIRACH VHGRFATKAN KRPSFTLKDA MENPQRDASR IVLPPASYAQ EQEKITERWP
AAVKFIQEHQ LNEFFAEGAK DFGIVMQGGL YNSVLRSLEL LGLADAFGNS QVPLYVLNLT
YPLIDDEFKR FCAGKRSILL VEEGQPDFIE QSVNSMLRKA DVQTKVHGKD VLPMAGEYTG
GVVLKGVARF IDIYAPELLQ GRELPVAARP ASSGLAVLDG NPKAFAIKAA SDEVQGRPPS
FCTGCPERPI FTAMKLIERE LGKHHISCDI GCHLFSILPP FNIGATTMGY GLGWAGASAF
NTPETSKRTI AMMGDGGFWH NGLTSGVGNA VFNQTDNVLL VVDNGYSAAT GGQDVLSSKS
SNPSLKPGST NNPIEKAVRG VGVKWAKTVT NTYSLTQMKD VLREALTTKE KGPKVIVAQS
ECMLNRQRRV KPQIRKRIEG GERVVRERFG IDPDTCTGDH SCIRLSGCPS LTIKPNPDPL
RRDPIATVID SCVGCGLCGE VAHAAVLCPS FYRAEIINNP TAWDRFKLRL RTAVISALQN
RIERRLEGIA A
//
