ID Q5LEP8_BACFN Unreviewed; 530 AA.
AC Q5LEP8;
DT 21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 21-JUN-2005, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE RecName: Full=Indolepyruvate oxidoreductase subunit IorA {ECO:0000256|PIRNR:PIRNR006439};
DE Short=IOR {ECO:0000256|PIRNR:PIRNR006439};
DE EC=1.2.7.8 {ECO:0000256|PIRNR:PIRNR006439};
DE AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit alpha {ECO:0000256|PIRNR:PIRNR006439};
GN ORFNames=BF9343_1621 {ECO:0000313|EMBL:CAH07402.1}, NCTC9343_03268
GN {ECO:0000313|EMBL:SUV39352.1};
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH07402.1, ECO:0000313|Proteomes:UP000006731};
RN [1] {ECO:0000313|EMBL:CAH07402.1, ECO:0000313|Proteomes:UP000006731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC Onslow {ECO:0000313|Proteomes:UP000006731};
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
RN [2] {ECO:0000313|EMBL:SUV39352.1, ECO:0000313|Proteomes:UP000255401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC9343 {ECO:0000313|EMBL:SUV39352.1,
RC ECO:0000313|Proteomes:UP000255401};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC of arylpyruvates. {ECO:0000256|PIRNR:PIRNR006439}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC (indol-3-yl)acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:12645, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17640,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57271,
CC ChEBI:CHEBI:57287; EC=1.2.7.8;
CC Evidence={ECO:0000256|PIRNR:PIRNR006439};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRNR:PIRNR006439};
CC Note=Binds 2 [4Fe-4S] clusters. In this family the first cluster has a
CC non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
CC {ECO:0000256|PIRNR:PIRNR006439};
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DR EMBL; CR626927; CAH07402.1; -; Genomic_DNA.
DR EMBL; UFTH01000001; SUV39352.1; -; Genomic_DNA.
DR RefSeq; WP_005786589.1; NZ_UFTH01000001.1.
DR PaxDb; 272559-BF9343_1621; -.
DR DNASU; 3286091; -.
DR GeneID; 66329476; -.
DR KEGG; bfs:BF9343_1621; -.
DR eggNOG; COG4231; Bacteria.
DR HOGENOM; CLU_017727_0_0_10; -.
DR OMA; IGDSTFM; -.
DR BioCyc; BFRA272559:G1GHZ-1737-MONOMER; -.
DR Proteomes; UP000006731; Chromosome.
DR Proteomes; UP000255401; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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; IPR045025; HACL1-like.
DR InterPro; IPR017721; IorA.
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; PF01855; POR_N; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR PIRSF; PIRSF006439; Indolepyruvate_ferr_oxidored; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|PIRNR:PIRNR006439};
KW Electron transport {ECO:0000256|PIRNR:PIRNR006439};
KW Iron {ECO:0000256|PIRNR:PIRNR006439};
KW Iron-sulfur {ECO:0000256|PIRNR:PIRNR006439};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR006439};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006439};
KW Pyruvate {ECO:0000313|EMBL:SUV39352.1};
KW Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT DOMAIN 15..181
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 380..513
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 530 AA; 58056 MW; 790B49C47633B508 CRC64;
MSKQLLLGDE AIAQAALDAG LSGVYAYPGT PSTEITEYIQ MAPITSERNI HNRWCANEKT
AMEAALGMSF VGKRALVCMK HVGMNVAADC FINSAITGVK GGLIVVAADD PSMHSSQNEQ
DSRFYGDFSL IPMYEPSNQQ EAYDMVYNGF EFSEKIGEPI LMRMVTRLAH SRSGVENKAQ
KPQNEISFSE DPRQFILLPG NARKRYKVLL TRQEEFIKAS EESPYNRYID GPNKKTGIVA
CGIGYNYLME NYPEGCEYPV LKVGQYPLPK KQLMQLIDAC DEILVLEDGQ PFVEKQLKGY
LGIGLKVKGR LDGTLSQDGE LNPDTVARAL GKENSSEFNV PNIVEMRPPA LCEGCGHRDM
YITLTQVLKE EYPTHKVFSD IGCYTLGANA PFNAINSCVD MGASITMAKG ASDGGLHPAV
AVIGDSTFTH SGMTGLLDCV NENANVTIVI SDNETTAMTG GQDSAGTGRL EAICAGLGVD
PAHIRVVVPL KKNYEEMKQI IREEINYKGV SVIIPRRECI QTLARKKRSK
//