UniProt: A0A174J138

Database: UniProt
Entry: A0A174J138_9BACE

LinkDB:  A0A174J138_9BACE 
Original site:  A0A174J138_9BACE

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (7)   
   EMBL (7)   
Protein domain (7)   
   InterPro (5)   
   Pfam (2)   
Literature (1)   
   PubMed (1)   
All databases (23)   

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ID   A0A174J138_9BACE        Unreviewed;       530 AA.
AC   A0A174J138;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=DWY26_02745 {ECO:0000313|EMBL:RGR73689.1}, DXA49_01485
GN   {ECO:0000313|EMBL:RGY29482.1}, ERS852494_01096
GN   {ECO:0000313|EMBL:CUO91976.1}, ERS852558_00749
GN   {ECO:0000313|EMBL:CUP67388.1}, F2Y31_06070
GN   {ECO:0000313|EMBL:KAA5501701.1}, F2Y35_05810
GN   {ECO:0000313|EMBL:KAA5493688.1}, F2Y36_05945
GN   {ECO:0000313|EMBL:KAA5464645.1};
OS   Bacteroides caccae.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=47678 {ECO:0000313|EMBL:CUO91976.1, ECO:0000313|Proteomes:UP000095657};
RN   [1] {ECO:0000313|Proteomes:UP000095657, ECO:0000313|Proteomes:UP000095725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5834880 {ECO:0000313|EMBL:CUO91976.1,
RC   ECO:0000313|Proteomes:UP000095657}, and 2789STDY5834946
RC   {ECO:0000313|EMBL:CUP67388.1, ECO:0000313|Proteomes:UP000095725};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000284205, ECO:0000313|Proteomes:UP000284431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF24-29LB {ECO:0000313|EMBL:RGR73689.1,
RC   ECO:0000313|Proteomes:UP000284205}, and OF02-6LB
RC   {ECO:0000313|EMBL:RGY29482.1, ECO:0000313|Proteomes:UP000284431};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000368418, ECO:0000313|Proteomes:UP000475905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIOML-A19 {ECO:0000313|EMBL:KAA5501701.1,
RC   ECO:0000313|Proteomes:UP000368418}, BIOML-A21
RC   {ECO:0000313|EMBL:KAA5493688.1, ECO:0000313|Proteomes:UP000491168},
RC   and BIOML-A31 {ECO:0000313|EMBL:KAA5464645.1,
RC   ECO:0000313|Proteomes:UP000475905};
RX   PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA   Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA   Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA   Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA   Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA   Xavier R.J., Alm E.J.;
RT   "A library of human gut bacterial isolates paired with longitudinal
RT   multiomics data enables mechanistic microbiome research.";
RL   Nat. Med. 25:1442-1452(2019).
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};
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DR   EMBL; CZAI01000002; CUO91976.1; -; Genomic_DNA.
DR   EMBL; CZBL01000002; CUP67388.1; -; Genomic_DNA.
DR   EMBL; VVYP01000005; KAA5464645.1; -; Genomic_DNA.
DR   EMBL; VVYF01000005; KAA5493688.1; -; Genomic_DNA.
DR   EMBL; VVYD01000003; KAA5501701.1; -; Genomic_DNA.
DR   EMBL; QRUO01000002; RGR73689.1; -; Genomic_DNA.
DR   EMBL; QSCS01000002; RGY29482.1; -; Genomic_DNA.
DR   RefSeq; WP_005677905.1; NZ_WQQZ01000013.1.
DR   STRING; 47678.ERS852494_01096; -.
DR   GeneID; 75113992; -.
DR   KEGG; bcac:CGC64_10500; -.
DR   Proteomes; UP000095657; Unassembled WGS sequence.
DR   Proteomes; UP000095725; Unassembled WGS sequence.
DR   Proteomes; UP000284205; Unassembled WGS sequence.
DR   Proteomes; UP000284431; Unassembled WGS sequence.
DR   Proteomes; UP000368418; Unassembled WGS sequence.
DR   Proteomes; UP000475905; Unassembled WGS sequence.
DR   Proteomes; UP000491168; 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:CUO91976.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095657};
KW   Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT   DOMAIN          15..181
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   530 AA;  58010 MW;  CAF09A372BFBCE89 CRC64;
     MSKQLLLGDE AIAQAALDAG LSGVYAYPGT PSTEITEYIQ MAPITTEQNI HNRWCTNEKT
     AMEAALGMSF VGKRALVCMK HVGMNVAADC FVNSAITGVK GGLIVVAADD PSMHSSQNEQ
     DSRFYGDFSL IPMYEPSNQQ EAYDMVYDGF EFSEKLGEPV LMRMVTRLAH SRSGVERKEQ
     KPQNGISFSD DPRQFILLPG NARKRYKVLL ARQDEFIKAS EESPYNKYTD GPNKKLGIIA
     CGIGYNYLME NYPEGCEYPV LKIGQYPLPK KQILQLVESC DEILVLEDGQ PFVEKQLKGY
     LGIGIKVKGR LDGTLSQDGE LNPDSVARAV GKENKSEFGI PSVVEMRPPA LCEGCGHRDM
     YITLTEVLKE EYPSHKVFSD IGCYTLGANA PFNAINSCVD MGASITMAKG AADGGLYPAV
     AVIGDSTFTH SGMTGLLDCV NENANVTIVI SDNETTAMTG GQDSAGTGRI EAICAGLGVD
     PAHIRVVVPL KKNYEEMKRI IREEIEYRGV SVIIPRRECI QTLARKKRSK
//

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