ID A0A370AS65_9SPIO Unreviewed; 530 AA.
AC A0A370AS65;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
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=DV872_16740 {ECO:0000313|EMBL:RDG30494.1};
OS Oceanispirochaeta sp. M1.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Oceanispirochaeta.
OX NCBI_TaxID=2283433 {ECO:0000313|EMBL:RDG30494.1, ECO:0000313|Proteomes:UP000253869};
RN [1] {ECO:0000313|EMBL:RDG30494.1, ECO:0000313|Proteomes:UP000253869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:RDG30494.1,
RC ECO:0000313|Proteomes:UP000253869};
RA Yadav S., Villanueva L., Damste J.S.S.;
RT "Draft genome sequence of Oceanispirochaeta sp. strain M1.";
RL Submitted (JUL-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};
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:RDG30494.1}.
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DR EMBL; QQPQ01000024; RDG30494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370AS65; -.
DR OrthoDB; 9804603at2; -.
DR Proteomes; UP000253869; 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:RDG30494.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253869};
KW Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT DOMAIN 15..191
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 381..516
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 530 AA; 57693 MW; E471E3858BB576A8 CRC64;
MSEYVVLGDE AVALGAVHGG VSSCYGYPGT PSTEIMEYLL EYSEKEDGPF ACWSSNEKTA
MEEALGTSFA GKRAIVTMKH VGLNVAADAF MNGALLDIRG GLVVVVADDP GMHSSQNEQD
TRFYADFAKI PLLEPANQQQ AYDMTREAFD LSEKMGCPVV LRLVTRLSHS RAAIVTKEAR
KENPINKADN KQDWMLLPAN ARRRWDSLLG RQKDMISYSE NSAINALTMN ESNKDRGIIT
TGLGYNYYKE NESELSDNPS HLHIGVYPVP EDKIRKIAAH VKELIILEEG YPLVERLIAG
LLPRDLKITG KLENIVPLQG ELNPDNIRPA LGLPARESAA PSTLDLVGRP PQLCKGCPHD
DTYRVIKEVQ AELEESTVTS DIGCYALGAL PPLSVPETII CMGASITAAK GSSEAGLNNV
MAVIGDSTFL HSGLTGLVDC VSSKTDVTII IVDNETTAMT GGQTTILPSS RLEGVVRGIV
GETDHVMTIP AHRKFHEENK EKLRKELAYK GVSVIIAVRE CIETARKAKK
//
