ID A0A3A9YVH3_9ACTN Unreviewed; 635 AA.
AC A0A3A9YVH3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=2-oxoacid:acceptor oxidoreductase subunit alpha {ECO:0000313|EMBL:RKN39227.1};
GN ORFNames=D7294_21885 {ECO:0000313|EMBL:RKN39227.1};
OS Streptomyces hoynatensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1141874 {ECO:0000313|EMBL:RKN39227.1, ECO:0000313|Proteomes:UP000272474};
RN [1] {ECO:0000313|EMBL:RKN39227.1, ECO:0000313|Proteomes:UP000272474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 29097 {ECO:0000313|EMBL:RKN39227.1,
RC ECO:0000313|Proteomes:UP000272474};
RX PubMed=24243968; DOI=10.1099/ijs.0.055640-0;
RA Veyisoglu A., Sahin N.;
RT "Streptomyces hoynatensis sp. nov., isolated from deep marine sediment.";
RL Int. J. Syst. Evol. Microbiol. 64:819-826(2014).
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:RKN39227.1}.
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DR EMBL; RBAL01000014; RKN39227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9YVH3; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000272474; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
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 InterPro; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR03710; OAFO_sf; 1.
DR PANTHER; PTHR32154:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000272474}.
FT DOMAIN 30..217
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 270..486
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 635 AA; 67905 MW; 3B16CB2BD9BDA60E CRC64;
MTTEVDRTSR DKKDVRRLDR VIIRFAGDSG DGMQLTGDRF TSETASLGND LSTLPNFPAE
IRAPAGTLPG VSSFQVHFAD HDILTPGDAP NVLVAMNPAA LKANVPDLPP GAEIIVNTDE
FNSRALAKVG YAGNPLEDGS LDAYHVHPVP LTTLTVEALK PFDLTRKEAG RSKNMFALGL
LSWMYHRPTE NTEAFLRAKF ARRPEIAEAN ITAFRAGWNF GETTEDFAVS YEVAPAASAF
PAGTYRNISG NLSLAYGLIA ASVRADLPLF LGSYPITPAS DVLHELSRHK NFGVRTFQAE
DEIAGIGAAL GASFGGSLGV TTTSGPGVAL KSEAIGLAVS LELPLLIIDI QRGGPSTGLP
TKTEQADLLQ AMFGRNGEAP VPIVAPATPA ECFDAALDAA RIALTYRTPV FLLSDGYLAN
GSEPWRVPEV DELPDLRVQF ATGPNVTLPD GGQAFHPYLR DPATLARPWA IPGTPGLEHR
IGGIEKQDGT GNISYDPANH DHMVRTRQAK VDGVTVPDVV VDDPSGPPGE GARVLVLGWG
STYGPITAAV RRIRREGGRI AQTHLRNLNP FPANLGEVLR AYDKVLLPEM NLGQLALLLR
AKYLVDVQSL TQVTGLPFKA EQLASAFKEA LDDDH
//
