ID   B2IB42_BEII9            Unreviewed;      1187 AA.
AC   B2IB42;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Pyruvate ferredoxin/flavodoxin oxidoreductase {ECO:0000313|EMBL:ACB93742.1};
GN   OrderedLocusNames=Bind_0083 {ECO:0000313|EMBL:ACB93742.1};
OS   Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB
OS   8712).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Beijerinckiaceae; Beijerinckia.
OX   NCBI_TaxID=395963 {ECO:0000313|EMBL:ACB93742.1, ECO:0000313|Proteomes:UP000001695};
RN   [1] {ECO:0000313|Proteomes:UP000001695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC   {ECO:0000313|Proteomes:UP000001695};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N.,
RA   Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.;
RT   "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC
RT   9039.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACB93742.1, ECO:0000313|Proteomes:UP000001695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC   {ECO:0000313|Proteomes:UP000001695};
RX   PubMed=20601475; DOI=10.1128/JB.00656-10;
RA   Tamas I., Dedysh S.N., Liesack W., Stott M.B., Alam M., Murrell J.C.,
RA   Dunfield P.F.;
RT   "Complete genome sequence of Beijerinckia indica subsp. indica.";
RL   J. Bacteriol. 192:4532-4533(2010).
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DR   EMBL; CP001016; ACB93742.1; -; Genomic_DNA.
DR   RefSeq; WP_012383100.1; NC_010581.1.
DR   AlphaFoldDB; B2IB42; -.
DR   STRING; 395963.Bind_0083; -.
DR   KEGG; bid:Bind_0083; -.
DR   eggNOG; COG1014; Bacteria.
DR   eggNOG; COG4231; Bacteria.
DR   HOGENOM; CLU_009166_1_0_5; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000001695; Chromosome.
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:ACB93742.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001695}.
FT   DOMAIN          741..926
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          958..1166
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1187 AA;  127791 MW;  3B3DE26E18150EE1 CRC64;
     MVKVAVNGET SRGNEPGSRT AWDPYDLTRE RLLLGGAQAV VRLLLMQKER DRRAGLKTAG
     FISGYRGSPL GGLDLQFVQA KKHFDAQDIH FQPGLNEDLA ATAVWGAQQA GLSGEGRFDG
     VFSLWYAKGP GVDRSGDALR HANLAGTASH GGVLALAGDD HTAESSSTAY QSEFAFIDAM
     IPVLAPANVQ EILDYGLLGL AMSRFTGTWV AMKCVKEIVQ ATSTVNASLD RIQPVLPTDY
     RLPPGGLGIR AGDIFLAQDE RLQTAKQEAL RAFLRANRLD RLIFNGGEAP RIGLIASGKT
     YLDLRQGLVH LGIENEDAAA ELGLRLYKVG CSWPLEPQGL RAFANGLDLI IVIEEKRALI
     EMQARDILYG MADHPFILGK QDRHGNSLFP ASGAYEASDI ALAIGDFLLD HGRRGPAKEL
     LAHRLETLRQ GSRLSARFTD VAQRLPGFCA GCPHNRSTQV PDGMRAYAGI GCHFMALGMD
     RSTQGFAHMG AEGANWIGEA PFSRRGHIIQ NLGDGTYTHS GLLAIRFAVA AGVDITYKIL
     FNDAVAMTGG QRLEGGPTVD RIARQLAAEG VAQIAVVTDE PEKYTPGIAW PAGVTIEPRQ
     ELDAVQRRLA TLPGVTVLLY DQTCATEKRR RGKRAKAAAP SRRVFINELL CEGCGDCGLV
     SNCVAIQPKE TEFGRKRTID QSSCNQDFSC LEGFCPALVS VEGVQPKRIA DTVADLFPAL
     PQPSLPVIGD RPFGIIVTGI GGTGVVTIGA LLGVAAHFEG KICGINDMAG LAQKGGAVFS
     HVRIAQAEDQ IHAIRIGQGE ADLVLGCDLV ATASRKILTA IVKGKTAVLV NDAEILPGDF
     ARDADYHLPA QACRQALLEA AGDGVTFIEA TNLATALFGQ SLAANLFLLG HAWQQGLVPL
     AENSILAAIA LNGQAVAMNE AAFLWGRRAA AHPASVAAII VKAQAKDGGR ILPVSTTLDQ
     IVSRRAAFLT AYQDEAYAER YLALVEQAIA TERRIMPGCD DFSKAVARNY FKLLAIKDEY
     EVGRLYSDGS FARQIGQTFE GEPVFTFYLR HPLWRRRVDE KGAEDKGKGT GNQPAKISLG
     PWMLPVFRLL ARLKVVRGTA FDLFGYQRER REERQMLADY ESTIADILSR LTPVNHSVAV
     ALAALPEKIR GFGPVRERHR QAAQAEEALL MRQLAASSAA TTLAAAE
//