ID A0A0P1H1N0_9RHOB Unreviewed; 1140 AA.
AC A0A0P1H1N0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=2-oxoacid ferredoxin oxidoreductase {ECO:0000313|EMBL:CUH88951.1};
GN ORFNames=PH5382_02895 {ECO:0000313|EMBL:CUH88951.1};
OS Phaeobacter sp. CECT 5382.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1712645 {ECO:0000313|EMBL:CUH88951.1, ECO:0000313|Proteomes:UP000050782};
RN [1] {ECO:0000313|EMBL:CUH88951.1, ECO:0000313|Proteomes:UP000050782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5382 {ECO:0000313|EMBL:CUH88951.1,
RC ECO:0000313|Proteomes:UP000050782};
RG Swine Surveillance;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CYSG01000013; CUH88951.1; -; Genomic_DNA.
DR RefSeq; WP_058335065.1; NZ_CYSG01000013.1.
DR AlphaFoldDB; A0A0P1H1N0; -.
DR STRING; 1712645.PH5382_02895; -.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000050782; 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:UP000050782}.
FT DOMAIN 727..913
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 936..1133
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1140 AA; 124686 MW; 3C3E975C5C478000 CRC64;
MTELSHEFRS YQLDDRYDNT TGRVFLTGTQ ALARIMLDQS RRDQSAGHKT AGFVSGYRGS
PLGAVDLEFW RSRKRMEEHR VKFMPAVNED LGATAVLGAQ QAILDPHCEV EGVFSMWYGK
GPGVDRSGDA LKHGNAYGSS SKGGVLVVAG DDHGCVSSSM PHQSDVAFMS WFMPVLNPAD
VSEFLSYGEY GFALSRYSGT WVGFKAVSET VESARSVELQ TDRDFTYPEL PEYPGGLHIR
RADLPSPEIE TRIRAKIKAV RAFAEANPID RRIYDVDAAK FGFVTTGKGH LDLMEALRLL
GLDEDACRAL GIDIYKVGMV WPLARPEALR FMRGKEEVLV VEEKRGIIES QFKEYFYDWP
GDKPNKMVGK YDSAGEPLIP WTGELSPLML APIVAARLDA FFPDQNLPAK AAALLAEPPK
LINVAGANRT PYFCSGCPHN TSTKLPEGSE AKSGIGCHVM ASWMDRDTAG YAQMGGEGVP
WTVASQFNGG KHVFQNLGEG TWYHSGSLAI RQAVAANTNI TYKILYNDAV AMTGGQPVDG
PVSVTGIAQT CRAEGVQRIA LVSDDIDKFH RGDFPSGTTF HDRADMDLVQ RELRDIKGVT
CLIYEQTCAT EKRRRRKRGA LEDPKKFAFI NDLVCEGCGD CSVESNCLSV EPKETAFGRK
RKINLSSCNK DFSCLNGFCP SFVTVEGGAR RKKLPAGLDR DALAAKLPAP ELPSLTEPFD
LLVTGVGGTG VVTVGALITM AAHLEGKGSS VLDFTGFAQK FGTVLSYIRL STSPESLNQV
RIDQAAADAV IGCDVVVSSA PKASAHYRAG TRIVLNRAEM PTGDLVLRRD ADLMAGLRER
EIAAAVGPEN LSGFNANEAA EALLGDAVLA NVMMLGFAWQ QGLVPVSGAA LDQAIELNGV
AIEKNRLAFT IGRAMAVDPD LVSQFYNEEA VAEETLEQII DRRAVFLTGY QDPAYAARYS
ETLAKFTSLL PLDAKEELTQ AAAKSLFKLM AYKDEFEVAR LMTGEGFKDQ IAEEFEGNYS
VNYHMAPPLL SRKKDARGRP VKKAFGPWLR PALSLLTRGK RLRGTPLNLF GYHEEARLHR
SLLAWYEAAL RTVANSYNGE KHRACLDILT APMEIRGYGP VRQDAAHKHR AAAERLLKQL
//
