ID A0A1G4VLM7_9FIRM Unreviewed; 572 AA.
AC A0A1G4VLM7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN02910339_01143 {ECO:0000313|EMBL:SCX08157.1};
OS Lachnospiraceae bacterium YSD2013.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520828 {ECO:0000313|EMBL:SCX08157.1, ECO:0000313|Proteomes:UP000199278};
RN [1] {ECO:0000313|EMBL:SCX08157.1, ECO:0000313|Proteomes:UP000199278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSD2013 {ECO:0000313|EMBL:SCX08157.1,
RC ECO:0000313|Proteomes:UP000199278};
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|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 ECO:0000256|PIRSR:PIRSR006439-50};
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, ECO:0000256|PIRSR:PIRSR006439-50};
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DR EMBL; FMTX01000011; SCX08157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4VLM7; -.
DR STRING; 1520828.SAMN02910339_01143; -.
DR OrthoDB; 9804603at2; -.
DR Proteomes; UP000199278; 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; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
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 NCBIfam; TIGR03336; IOR_alpha; 1.
DR PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR PANTHER; PTHR43710:SF5; INDOLEPYRUVATE FERREDOXIN OXIDOREDUCTASE ALPHA SUBUNIT; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF01855; POR_N; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR PIRSF; PIRSF006439; Indolepyruvate_ferr_oxidored; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|PIRNR:PIRNR006439, ECO:0000256|PIRSR:PIRSR006439-50};
KW Electron transport {ECO:0000256|PIRNR:PIRNR006439};
KW Iron {ECO:0000256|PIRNR:PIRNR006439, ECO:0000256|PIRSR:PIRSR006439-50};
KW Iron-sulfur {ECO:0000256|PIRNR:PIRNR006439, ECO:0000256|PIRSR:PIRSR006439-
KW 50};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR006439,
KW ECO:0000256|PIRSR:PIRSR006439-50};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006439};
KW Pyruvate {ECO:0000313|EMBL:SCX08157.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199278};
KW Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT DOMAIN 511..542
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 543..572
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 523
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 526
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 529
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 534
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 552
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 555
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 558
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 562
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
SQ SEQUENCE 572 AA; 62061 MW; 9CD1CC4CA526B324 CRC64;
MLGNAAIARG AYEAGVKVSA AYPGTPSTEI SENLVNYKEI YCEWSPNEKV ACEVAIGASM
AGARSMCSMK HVGLNVASDP LYSVSYIGVN GGMVLVVADD PGLYSSQNEQ DTRMIGRASM
VPVIEPSDSQ EAKDYIKYAF ELSEKYDTPV IMRTTTRLGH SQGLVTLEER QEIPDKPYEK
NIQKNVMMPG MAKKRHVFVE ERLKKMAEDG ASMPINRIEW GDKKLGFITS GIAYQYVKEV
CPDASVLKLG LLNPLPKTLI ADFAKEIETL YIFEELEPVI EEQVRAMGIK CIGKEAFTIQ
GEYSANMLRK VLKGSEPETK AQEVPARPPI LCPGCPHRSV YTALKNLKIH AAGDIGCYTL
GAVAPLNVVD TAVCMGSSIS TLHGMEKAKG KDYVKNWVAV IGDSTFLHTG VNSLMNMVYN
KATGTVMILD NSTTGMTGHQ DHAATGKTLM GEPTYAIDIY NLCKSMGIEH VVEVSSFDQA
GLTKAIKEET ARDEVSVIIC QAPCALLKGQ KFPNVCKPVS DKCKKCGACL KPGCPALTKN
ADGTVSIDVT MCNGCGLCKQ MCKFDAIECV ER
//
