ID   A0A086W5S1_9BURK        Unreviewed;      1185 AA.
AC   A0A086W5S1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:KFI05121.1};
DE            EC=1.2.7.8 {ECO:0000313|EMBL:KFI05121.1};
GN   ORFNames=JN27_21865 {ECO:0000313|EMBL:KFI05121.1};
OS   Massilia sp. BSC265.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1549812 {ECO:0000313|EMBL:KFI05121.1, ECO:0000313|Proteomes:UP000028843};
RN   [1] {ECO:0000313|EMBL:KFI05121.1, ECO:0000313|Proteomes:UP000028843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSC265 {ECO:0000313|EMBL:KFI05121.1,
RC   ECO:0000313|Proteomes:UP000028843};
RA   Kellom M., Bailey A., Poret-Peterson A., Noonan K., Raymond J.;
RT   "Draft Genome of Massilia consociata BSC265, Isolated from Biological Soil
RT   Crust of Moab, Utah.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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:KFI05121.1}.
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DR   EMBL; JPXI01000042; KFI05121.1; -; Genomic_DNA.
DR   RefSeq; WP_036252966.1; NZ_JPXI01000042.1.
DR   AlphaFoldDB; A0A086W5S1; -.
DR   STRING; 1549812.JN27_21865; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000028843; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR046667; DUF6537.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR   PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   Pfam; PF20169; DUF6537; 1.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KFI05121.1}; Pyruvate {ECO:0000313|EMBL:KFI05121.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028843};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          483..633
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   DOMAIN          760..933
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          975..1173
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
SQ   SEQUENCE   1185 AA;  129279 MW;  9EBFC4A32AF2F58C CRC64;
     MPDTVTPQAV TPDYSSRLNT VTLDDKYTAK SGNIFLSGIQ ALVRLPMMQR ERDAAAGLNT
     AGFVSGYRGS PLGGLDETLW KAKGHLEANH VQFVPGVNED LAATAVWGTQ TVDLIGPAKY
     DGVFAMWYGK GPGVDRCGDV FKHMNHAGTS KHGGVLLVAG DDHGAYSSTL PHQSDHIFSA
     CMIPVLYPCN VQEYLDLGVH GWAMSRYSGC AVAFKALADT VESSASVDAN PFRVEVKYPQ
     DFAMPEGGLN TKLSSVPLGQ QARAQEALMQ DYKIYAALAY ARENKLNRTT IDSPNAKLGI
     IASGKSYLDV LEALEELGID EAMAEKVGLR LYKVAMIWPL EPEGVREFAQ GLEEILVVEE
     KRQVVEYQLK EQLYNWRDDV RPHIVGKFDD KGEWVAPRGD WLLPPKADFS VAQVARVIAG
     RIARLVTDEP TRDLIKARLS FLEAKDAVLQ KAITTPFRPA FYCSGCPHNT STKVPDGSFA
     LAGIGCHVMA TSIYPEMNKL TTHMGGEGTP WIGQAAFSKV PHVFQNLGDG TYFHSGYLAI
     RAAVSAKVNI TYKILYNDAV AMTGGQPVDG TTSVPHIAQQ MAAEGVKRIA LVTEDLSRYA
     DRSNLPAMVT LHDRKHMDEV QRELRELPGV TVIIYDQTCA AEKRRRRKKN EFPDPNQRMV
     INEAVCEGCG DCGIQSNCVS ILPKETEFGR KRQIDQSSCN KDYSCAKGFC PSFVTVEGGT
     LKKSKTGVST NGSEDGWGAL PEPVLPSVEH PYNILINGIG GTGVITVGAL MGMAAHLEGK
     GASVLDMTGM SQKNGSVTSH VKIAATPDRL RAQRIATGEA DLILGCDILT TGAADAVSKM
     RPGRTLAIVN LHEQPTGTFA QQRDWEFPSG DVRSLILEAV GGESGADFVD ATKLATALMG
     DSIATNLFLM GYAWQKGRIP LSEAALLRAI ELNGVAVASN KMSFLWGRRA AVDFKRVEKQ
     AIPAQTVVIQ MPHSLDSVIK RRVEHLTGYQ DAAYAAVYED LVKRVREAET AKGLGNKLSM
     AVARNYAKLM AYKDEYEVAR LYTDGRFIEQ LKTQFEGDVK LKFNLAPPLF AKKDAKGHMV
     KAQYGSWMFG AFKLLAKMKG LRGGVFDLFG RTAERKMERA LIGEYREMVE ALVARLDASN
     HADAVELASL PEQIRGFGHV KEKAVAEFHA RKAELLSGNI KRRAA
//