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Database: UniProt
Entry: A0A0Q6WG56_9BURK
LinkDB: A0A0Q6WG56_9BURK
Original site: A0A0Q6WG56_9BURK 
ID   A0A0Q6WG56_9BURK        Unreviewed;      1178 AA.
AC   A0A0Q6WG56;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Pyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:KQV84621.1};
GN   ORFNames=ASD15_05395 {ECO:0000313|EMBL:KQV84621.1};
OS   Massilia sp. Root351.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV84621.1, ECO:0000313|Proteomes:UP000051876};
RN   [1] {ECO:0000313|EMBL:KQV84621.1, ECO:0000313|Proteomes:UP000051876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root351 {ECO:0000313|EMBL:KQV84621.1,
RC   ECO:0000313|Proteomes:UP000051876};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV84621.1, ECO:0000313|Proteomes:UP000051876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root351 {ECO:0000313|EMBL:KQV84621.1,
RC   ECO:0000313|Proteomes:UP000051876};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQV84621.1}.
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DR   EMBL; LMDJ01000012; KQV84621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q6WG56; -.
DR   Proteomes; UP000051876; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
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; -; 1.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
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; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   PANTHER; PTHR48084:SF1; 2-OXOGLUTARATE SYNTHASE SUBUNIT KORB; 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.
DR   PROSITE; PS51379; 4FE4S_FER_2; 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   Pyruvate {ECO:0000313|EMBL:KQV84621.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051876};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          640..670
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1178 AA;  127561 MW;  4C1BC99F29AEC501 CRC64;
     MNSMTLPASI QPALADPDYA LSDNLTRTQG RVFLTGTQAL VRLLCMQKIC DDAQGLNTGG
     FVSGYRGSPL GAVDQELWRA SRLLAKHNVE FLPAINEELG ATAVLGSQQV EADPTRKVDG
     VFAMWYGKGP GVDRAGDALK HGHVYGSSPR GGVLVILGDD HGCVSSSMPH QSEQALIAWS
     MPVINPANIQ EYLEFGLYGW ALSRYSGAWS GFKAISETVE GGAVVELPPL PSYVMPTDYT
     APPDGLHNRW PDLPGLALEV RAAEKLEAVQ AFARANSIDR LVVPAPRAAV GIISAGKAYL
     DLLEALERLG LPLRRLEELG VRLYKPGLTY PLERTRLAAF ADGLQEILVV EEKGAVIEQQ
     VKNLFYNLPQ SERPAVIGKT DRNGDALLSA LGELRPSRIA PAIVQWLAPR FPELDLKRML
     PDFCAAELLS NSADGIKRTP YFCSGCPHNT STRVPEGSRA MAGIGCHFMA TWMKRDTNYL
     AQMGGEGISW VGSSRFVGEK HVFQNLGDGT YYHSGSLAIR QAIAARTNIT YKILYNDAVA
     MTGGQPVDGT LSVPQIVQQV VSEGAKKVVV VTDQPENYTG VALPAGVTVH HRSELDAMQR
     MLREIAGVTV LVYDQTCAAE KRRRRKKNKP EKIVFPDPAR RMVINPAVCE GCGDCGVQSN
     CLSILPLETE LGRKRQIEQS SCNKDYSCVE GFCPSFVSVL GGTLRKPASV ALTLADLEQA
     LGRYPAPAPH ALDKPFEILV AGVGGTGIVT VGALITMAAH LEGKGASTLD FMGFAQKGGA
     VLSHVRVAAS PSALNQVRID LQQADAVFAC DLVVAAMPDS LSVMRRGHTQ VVANEREIPT
     AEFTRDRDAS INKDGLLEKL ASAAGGANLL QLDAQEIAAR FLGDPIGGNI LLMGYAWQKG
     LVPAGLEALM RAIELNGVAI DMNKRAFMLG RLAAADQDAL SRLAQPQQQV IQFAAPKSLP
     ELVAFRADWL SKYQNAAYAR VYADAVAAVE LKEVALDGDG AKRTLSKAVA RNLFKLMAYK
     DEYEVARLHA DPSFREQIAA RFEGDYKLGF HLAPPLLARK KPGSDVPAKM AFGGWMMKGF
     GGLARLKCLR GTPLDIFGYT EERRRERALR DRYLAFVHEL SACLGLHNKA AALRLAQLPE
     QVRGYGHVKL AAMDQVDAAW QARMVEFQTP ATELKRQA
//
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