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Database: UniProt
Entry: A0A101VBX0_9FIRM
LinkDB: A0A101VBX0_9FIRM
Original site: A0A101VBX0_9FIRM 
ID   A0A101VBX0_9FIRM        Unreviewed;       192 AA.
AC   A0A101VBX0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Indolepyruvate oxidoreductase subunit IorB {ECO:0000256|ARBA:ARBA00017709};
DE            EC=1.2.7.8 {ECO:0000256|ARBA:ARBA00012812};
DE   AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit beta {ECO:0000256|ARBA:ARBA00033011};
GN   ORFNames=APF76_13380 {ECO:0000313|EMBL:KUO51673.1};
OS   Desulfitibacter sp. BRH_c19.
OC   Bacteria; Bacillota; Clostridia; Moorellales; Desulfitibacteraceae;
OC   Desulfitibacter.
OX   NCBI_TaxID=1734395 {ECO:0000313|EMBL:KUO51673.1, ECO:0000313|Proteomes:UP000053015};
RN   [1] {ECO:0000313|EMBL:KUO51673.1, ECO:0000313|Proteomes:UP000053015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c19 {ECO:0000313|EMBL:KUO51673.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC       of arylpyruvates. {ECO:0000256|ARBA:ARBA00002995}.
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|ARBA:ARBA00033657};
CC   -!- SUBUNIT: Heterodimer of the IorA and IorB subunits.
CC       {ECO:0000256|ARBA:ARBA00011238}.
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:KUO51673.1}.
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DR   EMBL; LOER01000023; KUO51673.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101VBX0; -.
DR   STRING; 1734395.APF76_13380; -.
DR   Proteomes; UP000053015; Unassembled WGS sequence.
DR   GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR017719; Indolepyruvate_Fd_OxRdtase_bsu.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   NCBIfam; TIGR03334; IOR_beta; 1.
DR   PANTHER; PTHR43854; INDOLEPYRUVATE OXIDOREDUCTASE SUBUNIT IORB; 1.
DR   PANTHER; PTHR43854:SF1; INDOLEPYRUVATE OXIDOREDUCTASE SUBUNIT IORB; 1.
DR   Pfam; PF01558; POR; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:KUO51673.1}.
FT   DOMAIN          12..189
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
SQ   SEQUENCE   192 AA;  21158 MW;  2CF68F4405050EEE CRC64;
     MADKSILIVG VGGQGTLLAS KVLGQVVMQE GLDIKMSEVH GMAQRGGSVV TQVRFGEKIY
     SPLIPDEGAD IILSFEMMEA LRYLPLLKKD GKIIINEQKI APMPVLVGAV KYPEDPIKEI
     QKMGIEVIGL KAYELAKEAG NMKAANVVLL GVLAKDLDFD ENMWENAIKE TVPERFLEVN
     MKAFEMGYNY NI
//
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