ID A0A124PB21_9BURK Unreviewed; 1191 AA.
AC A0A124PB21;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Pyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:KVE33439.1};
GN ORFNames=WS68_12510 {ECO:0000313|EMBL:KVE33439.1};
OS Burkholderia sp. TSV86.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1385594 {ECO:0000313|EMBL:KVE33439.1, ECO:0000313|Proteomes:UP000066043};
RN [1] {ECO:0000313|EMBL:KVE33439.1, ECO:0000313|Proteomes:UP000066043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSV86 {ECO:0000313|EMBL:KVE33439.1,
RC ECO:0000313|Proteomes:UP000066043};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
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:KVE33439.1}.
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DR EMBL; LOWB01000109; KVE33439.1; -; Genomic_DNA.
DR RefSeq; WP_059572524.1; NZ_LOWB01000109.1.
DR AlphaFoldDB; A0A124PB21; -.
DR Proteomes; UP000066043; Unassembled WGS sequence.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; 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; 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 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 SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:KVE33439.1}.
FT DOMAIN 739..925
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 954..1150
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1191 AA; 128031 MW; 83F88E37D7EA3D73 CRC64;
MNARLPVGSP PVLADYRLSD NLCATRGRIF LTGTQALVRI LLMQRALDAD AGLNTAGFVS
GYRGSPLGMV DQQLWKAKKL LDAGGVRFLP AINEELGGTA VLGTQRVEAD PERTVDGVFA
MWYGKGPGVD RAGDALKHGN AYGASPHGGV LVVAGDDHGC VSSSMPHQSD FAMIAWHMPI
VNPANIGEML EFGLYGYALS RFSGAWVGFK AISETVESAS SVDLDTLATR WPAPVDYVPP
ADGLHNRWPD LPSLAIEARL AAKLGAVRHF ARTNSIDKWI AASAHANVGI VTCGKAHLDL
MEALRRLDLT VADLDAAGVR IYKVGLSFPL ETTRLDAFVD GLAEVLVIEE KGPVVEQQIK
EHLYNRAPEA RPAVIGKRDA SGAPLLPELG ELRPSRILPV FADWLARHKP ALDRRARVVD
LVAPRILSNH ADAVRRTPYF CSGCPHNTST RVPEGSVAQA GIGCHFMASW MERGTTGLIQ
MGGEGVDWAA HAMFTNTRHV FQNLGDGTYF HSGILAIRQA VAARANITYK ILYNDAVAMT
GGQPVDGSIS VPQIARQVEA EGVSRFVVVS DEPQKYDGHH AQFPAGTTFH HRSELDAVQR
ELRDTPGVTV LIYDQTCAAE KRRRRKKGEY PDPDRRLFIN EAVCEGCGDC GVQSNCLSVE
PVETALGRKR RIDQSSCNKD FSCVNGFCPS FVTVEHAQLK KAAGAAFDEA ALAARVDALP
RPATHLDAAP FDLLITGVGG TGVVTIGALV SMAAHLEGKS ASVLDFMGFA QKGGAVLSFV
RIASSPVWLN QARIDTQQAD VLLACDMVVG ASADALQTVR RARTRIVVNT HAIPNAAFVR
DPDASLHADA LLEKMRDAAG DAFLTRCDAQ ALATKFLGDT VGANVLMLGF AWQQGNVPVS
LDAMMRAIEL NGVAVPMNKL AFSIGRMVAG DAAGLDALWN ARHPVHEPLP PLTLDALVAD
RIERLAAYGG ARYAERYRAL VDAARATGDE RVARAVATTF HRLLAVKDEY EVARLYTNGA
FRAALEAQFE GVAGKDFRVR FHLAPPAIAK AGKDGGAPRK RAFGQWLWPA LGMLARVRGL
RGTPLDPFGR TLERKMERAF ADDYETTMRR ALAAFTPQTA DTVVRLAELH AKARGYGHVK
FANVAGVKRT ERELAARLTI EAATSAAVTR ALDTFKGAGA LRGIPVVVAK S
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