ID A0A2I0N3M3_9CLOT Unreviewed; 595 AA.
AC A0A2I0N3M3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=ABB02_00075 {ECO:0000313|EMBL:PKK40626.1};
OS Clostridiaceae bacterium JG1575.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae.
OX NCBI_TaxID=1658742 {ECO:0000313|EMBL:PKK40626.1, ECO:0000313|Proteomes:UP000237298};
RN [1] {ECO:0000313|EMBL:PKK40626.1, ECO:0000313|Proteomes:UP000237298}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG1575 {ECO:0000313|EMBL:PKK40626.1,
RC ECO:0000313|Proteomes:UP000237298};
RA Nelson M.C., Graf J.;
RT "Draft genome of Clostridiaceae bacterium JG1575.";
RL Submitted (OCT-2015) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK40626.1}.
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DR EMBL; LQGW01000005; PKK40626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0N3M3; -.
DR OrthoDB; 9804603at2; -.
DR Proteomes; UP000237298; 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; IPR017900; 4Fe4S_Fe_S_CS.
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:SF7; INDOLEPYRUVATE OXIDOREDUCTASE SUBUNIT IORA; 1.
DR Pfam; PF13237; Fer4_10; 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; PS00198; 4FE4S_FER_1; 1.
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|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR006439};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRNR:PIRNR006439};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR006439};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006439,
KW ECO:0000313|EMBL:PKK40626.1}; Pyruvate {ECO:0000313|EMBL:PKK40626.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000237298};
KW Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT DOMAIN 535..563
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 565..594
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 544
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 547
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 550
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
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 574
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 577
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 580
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 584
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
SQ SEQUENCE 595 AA; 65385 MW; AB22CD24116BC57A CRC64;
MKELMTGNEA LARGAYEAGV RFASAYPGTP STEILENTAL YKESIVAQWA NNEKVALEAA
AGASVAGARA FAAMKHVGVN VAADPLFTFA YTGVNGGFVL ITADEPGQHS SQNEQDNRNY
AKFAKIPCIE PKDAQECKDF MKRAFELSEA YDTPVLLRVT TRVCHSKGIV DLAERKEVPI
KEYQKDAKKY VTVPAHARIL RAKVEERLQK LARFANETAL NRIEYHSKKI GVVASGSCID
YAREVFGEEA SYLMIGFSFP MPTEKMKEFA KEVETLYVIE ENDPIIEEEM QRLGLTVHGK
DTFPAFGELT PDVLRQALYG KTLDAVTAST EHVVPRPPSL CAGCPHRGLF YEIGKLKNTM
ISGDIGCYTL GFAEPYNAMD INLCMGAGIS VGHGAQTVFD MDPENKKRVI TVMGDSTFFH
TGVNSLINTA YNGSNTINII LDNRITGMTG HQENPGSGYT LQGKKTQEVD LTALVKACGI
EHVITINPND LAAVKNAVKW AESLEAPSVI ITRWPCVLKK LHEEDKAEFV NVFKEKCYVD
QDTCIGCRAC TRTGCPAIEF DYEKKKSFIN RNACVGCTVC LQVCPVKAIK KEGKN
//
