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Database: UniProt
Entry: A0A1Y4CXC2_9BACT
LinkDB: A0A1Y4CXC2_9BACT
Original site: A0A1Y4CXC2_9BACT 
ID   A0A1Y4CXC2_9BACT        Unreviewed;       532 AA.
AC   A0A1Y4CXC2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=B5F77_12050 {ECO:0000313|EMBL:OUO50832.1};
OS   Parabacteroides sp. An277.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=1965619 {ECO:0000313|EMBL:OUO50832.1, ECO:0000313|Proteomes:UP000196154};
RN   [1] {ECO:0000313|Proteomes:UP000196154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An277 {ECO:0000313|Proteomes:UP000196154};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUO50832.1}.
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DR   EMBL; NFJB01000031; OUO50832.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4CXC2; -.
DR   OrthoDB; 9804603at2; -.
DR   Proteomes; UP000196154; 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:OUO50832.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196154};
KW   Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT   DOMAIN          15..187
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   532 AA;  58251 MW;  FADBB48C0DB99A5F CRC64;
     MGKYLFLGDE AIAQAAIDAG LSGVYAYPGT PSTEITEYIQ ASSVAKERNI HCQWSANEKT
     AMEAALGMSY AGKRSLCCMK HVGMNVAADC FMNAAMSGIN GGMIIVTADD PSMHSSQNEQ
     DNRMYGNFAM IPMLEPSSQQ EAYDMVYEGF ELSEKLGYPI LLRVTTRMAH SRAGVETREL
     KDTLPMHCPE DGRQRYILLP ALARQRYRKL IAAQEAFEQS SEASLYNVYY DAPDKSLGII
     ATGIAFNYLS ENYPEGFKHP VLKISQYPVP TEKLARLVDE CEEILVLEEG YPVVEQQLKG
     LLSKGLKVHG RLDGTLQRDG ELTPDAVGKA LGLNITQYYA TPEVVEQRPP ALCQGCGHRD
     MYQALNEVLA EYEGAKVFGD IGCYTLGALP PFRAIDTCID MGASITMAKG ASDAGVFPAV
     SVIGDSTFTH SGMTGLLDCV NENTNITIVI SDNETTAMTG GQDSAGTGRL ESICTGIGVD
     PAHIRVMIPL KKNYEEMKQI IREEIEYRGV SVLIPRRECI QTLTRKKKAS KK
//
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