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
//