ID A0A238KL70_9RHOB Unreviewed; 1143 AA.
AC A0A238KL70;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=2-oxoacid ferredoxin oxidoreductase {ECO:0000313|EMBL:SMX42776.1};
GN ORFNames=PEV8663_02472 {ECO:0000313|EMBL:SMX42776.1};
OS Pelagimonas varians.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pelagimonas.
OX NCBI_TaxID=696760 {ECO:0000313|EMBL:SMX42776.1, ECO:0000313|Proteomes:UP000220836};
RN [1] {ECO:0000313|EMBL:SMX42776.1, ECO:0000313|Proteomes:UP000220836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8663 {ECO:0000313|EMBL:SMX42776.1,
RC ECO:0000313|Proteomes:UP000220836};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FXYH01000008; SMX42776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238KL70; -.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000220836; 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:UP000220836}.
FT DOMAIN 727..900
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 938..1137
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1143 AA; 124486 MW; FE40CC894EDCF508 CRC64;
MTDQTPILKD YELTDRYTKT SGRVFLTGTQ AIVRIALDQA RRDKVAGLDT RGYVSGYRGS
PVGGIDLEIG RNAKLVADAG VEFLPAVNEE FGATQMIGTQ QVETDPDKQV EAVFGLWYGK
GPGVDRAADA LKHGNAYGSS PKGGVLVVAG DDHGCVSSSM PHQSDVAFMN FFMPNINPAN
IAEFLPFAEW GYALSRFSGM WVGFKAISET VESGMSFELP TDREFVAPDY TAPETGLHYR
WPDLPGPQIE ERMEAKKEAV LAFARANPID RVEWGHSDAR FGIVTTGKAH LDVLEALRLL
GIDQAQACDL GLDIYKVGMV WPLEDVGALQ FASGKQELLV IEEKRGIIES QLKEYFYDFP
GQKPQRMVGK RDENGTRLIP WTHELGAVML AKIIAARLDL NFGLELSTKA NAIVPAPNLI
TVDGATRTPY FCSGCPHNTS TKVPEGSQAM AGIGCHFMAS WMDRNTTSLI QMGGEGVNWV
ARSKFNGNKH VFQNLGEGTY YHSGSLAVRQ AIAAGTNITY KILFNDAVAM TGGQTVDGPI
EVTSIAKSMV AEGAVKVVVV SDVPEQFSKS DFPDGVEILH RSEMDRIQRQ LREIPGTTIL
IYQQTCATEK RRLRKRGKLE DPKKFAVINP LVCEGCGDCG VESNCLSIEP LETEFGRKRR
INLNSCNKDF TCVNGFCPSF VTVEGGTLKK PSAEGKKVEF DRLKTQLTAP VLPSLDTPFD
ILVTGVGGTG VVTVGQLIAM AANLEGKGAS VLDFMGFAQK FGPVLSYIRM GNTEAEVNQA
RIEPSSANAL IGCDLVVSSS PKASATYRKG HTRAVVNTAL MPTGDFTRNR DTDLRASDRV
NRIADGVDAA SLRSLDANAL SQALMGDTVY ANVLMLGAAW QAGLVPLSEM ALMRAIDLNG
VKPAQNKDAF TWGRICVAAP DQATQVADLP ETPVHSLTEM VSRRADFLTD YQDAQWAQAY
QQAITEVMDA EQKTIGHTGP LSEAAAKGLF KLMSYKDEYE VARLHLETGF LEGLQQQFEG
DFTVKHHLAP PLLSGKPDAR GRPVKRAFGP WVRVGFKGLA RMKTLRGGAF DVFGKTAERK
MERTLITEYR DLLQGLTKGL TKDNHTQAAR IAGLVMDIRG FGPVKEQAVQ EVRTQIATDM
AQF
//
