ID   B6BC28_9RHOB            Unreviewed;      1140 AA.
AC   B6BC28;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=2-oxoacid:ferredoxin/flavodoxin oxidoreductase, gamma subunit domain protein {ECO:0000313|EMBL:EDZ48631.1};
GN   ORFNames=RBY4I_3854 {ECO:0000313|EMBL:EDZ48631.1};
OS   Rhodobacterales bacterium Y4I.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX   NCBI_TaxID=439496 {ECO:0000313|EMBL:EDZ48631.1, ECO:0000313|Proteomes:UP000005133};
RN   [1] {ECO:0000313|EMBL:EDZ48631.1, ECO:0000313|Proteomes:UP000005133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4I {ECO:0000313|EMBL:EDZ48631.1,
RC   ECO:0000313|Proteomes:UP000005133};
RA   Moran M.A., Buchan A., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; DS995281; EDZ48631.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6BC28; -.
DR   STRING; 439496.RBY4I_3854; -.
DR   eggNOG; COG1014; Bacteria.
DR   eggNOG; COG4231; Bacteria.
DR   HOGENOM; CLU_009166_1_0_5; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000005133; 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   Reference proteome {ECO:0000313|Proteomes:UP000005133}.
FT   DOMAIN          727..913
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          936..1134
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
SQ   SEQUENCE   1140 AA;  124449 MW;  A6AA86056AAAEC4B CRC64;
     MTKLSHDFRS YKLDDRYEMT KGRVFLTGTQ ALARVMLDQA RRDREAGLNT AGFVSGYRGS
     PLGGVDLEFW RAKARMEENR IKFMPAVNED LGATAVLGAQ QAVLDPHCEV EGVFSMWYGK
     GPGVDRSGDA LKHGNAYGSS PKGGVLVVAG DDHGCVSSSM PHQSDVAFMS WFMPVLNPAD
     VSEYLTFGEY GFALSRYSST WVGFKAVSET VESARSVELQ PDREFVFPEL PDYPGGLHIR
     RADLPSPEIE TRIQAKLDAV RAFAEANPID KRIYDIKEAR FGFISTGKGH LDLMEALRLL
     GLDEAACRRL GIDIYKVGMV WPLDRTDALK FVKGKQEVLV VEEKRGIIES QFKENFYDWP
     GSKPERMVGK YDSQGEPLIP WTGELSPLLL APIVAARLDK FFPEENLPAK AAALTAEPPK
     VLNVPGATRT PYFCSGCPHN TSTKLPEGSK AFSGIGCHVM ASWMDRETAG YAQMGGEGVP
     WTVASQFNGN KHVFQNLGEG TWYHSGSLAI RQAVAAGTNI TYKILYNDAV AMTGGQPVDG
     PVSVHGIAQT CRAEGVERIA LVSDNIGKFS RGDFPAGTTF HDRSALDSVQ RELRDIPGVT
     VLIYEQTCAT EKRRRRKRGK MEDPAKFAFI NDLVCEGCGD CSVESNCLSV EPKETPFGRK
     RKINLSTCNK DFSCLNGFCP SFVTVEGAAR RKKKIAGLDA AALTAKLPAP GLPALKEPFD
     LLVTGVGGTG VVTVGALITM AAHLEGKGAS VLDFTGFAQK FGTVLSYIRL SAAPDTLNQV
     RIDQGGADAV IGCDVVVSSA PKASVHYRAG TRVVLNRAEM PTGDLVLRRD ADLMAGVRER
     TIAEAVGPQN LSGFNANEAA EKMLGDAVLA NVMMLGFAWQ KGLVPVSAGA LDQAIELNGV
     AIDKNRLAFA IGRAMAVDPG LVASHYEEAP QREETLDELI ERRATFLTGY QNMAYASRYT
     AALNRFRAAL PHDAQEELTA AAARSLFKLM AYKDEYEVAR LLTSDGFQHQ LEEEFEGDFS
     VKYHLAPPLM NWKRDARGRP AKRVFGAWMR PAMNLLAKGK ALRGSAFNIF GYHEEARLHR
     DLLAWYEGVL DTVAGRYGAD KRKQSLELLK APMEIRGYGP VRLQAAKDVR AKAEEALSSL
//