ID A0A1G8M654_9RHOO Unreviewed; 543 AA.
AC A0A1G8M654;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Indolepyruvate oxidoreductase subunit IorA {ECO:0000256|ARBA:ARBA00017710, ECO:0000256|PIRNR:PIRNR006439};
DE Short=IOR {ECO:0000256|PIRNR:PIRNR006439};
DE EC=1.2.7.8 {ECO:0000256|ARBA:ARBA00012812, ECO:0000256|PIRNR:PIRNR006439};
DE AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit alpha {ECO:0000256|ARBA:ARBA00030514, ECO:0000256|PIRNR:PIRNR006439};
GN ORFNames=SAMN05660652_03770 {ECO:0000313|EMBL:SDI63401.1};
OS Propionivibrio dicarboxylicus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Propionivibrio.
OX NCBI_TaxID=83767 {ECO:0000313|EMBL:SDI63401.1, ECO:0000313|Proteomes:UP000198607};
RN [1] {ECO:0000313|EMBL:SDI63401.1, ECO:0000313|Proteomes:UP000198607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5885 {ECO:0000313|EMBL:SDI63401.1,
RC ECO:0000313|Proteomes:UP000198607};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC of arylpyruvates. {ECO:0000256|ARBA:ARBA00002995,
CC 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|ARBA:ARBA00033657,
CC 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};
CC -!- SUBUNIT: Heterodimer of the IorA and IorB subunits.
CC {ECO:0000256|ARBA:ARBA00011238}.
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DR EMBL; FNCY01000024; SDI63401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8M654; -.
DR STRING; 83767.SAMN05660652_03770; -.
DR OrthoDB; 9804603at2; -.
DR Proteomes; UP000198607; 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 InterPro; IPR009014; Transketo_C/PFOR_II.
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.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRNR:PIRNR006439};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR006439};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR006439};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRNR:PIRNR006439};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR006439};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR006439}; Pyruvate {ECO:0000313|EMBL:SDI63401.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198607};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR006439}.
FT DOMAIN 20..177
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 363..511
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 543 AA; 57495 MW; D4DE954110EBBEE0 CRC64;
MVAKLADRML LSGDEAVALA AFNAGVLLGT GYPGTPSTEI LEAFAALGGK AQWAPNEKVA
LEVGIGVAFA GGRSLVTMKH VGVNVAADAL FTAAYTGVTG GLVLVSADDP GMASSQNEQD
NRHYARAAGL LMLEPADSQQ AYDFAAAAFA LSEQFRQPVL LRMTTRTCHS KSIVTQTALP
GPAQAPSFER NIPARVMIPA YARPAHHALR DKLARAAAYA ENCAQTIVEP RSKALGIIAS
GVAAMHAREV APEASLLQLG FSYPLPMQAI RDFVASVERC VVIEEGDRIL VTELRAEGLA
VEGKPERFRF GELNADRVRR ILEHDDSPEA KIPGGKPPAL CEGCSHRPVF EALNRLDCIV
SGDIGCYSLG VLPPFTAMDT LVCMGASIGV GLGMRHVLPP EQAKRVVSVI GDSTFVHSGL
TGLAEMVYNP PPTGHVVLIV DNGTTAMTGQ QEHPGTGRTL LHDATGRLLF EDIARAMGIA
DVITVDPMAS DVVLDDVLRQ ALDSGRLVVI VARRPCILAA PKIRQYERAA AEKRIGIAVR
VDG
//
