ID A0A0F7CNV2_9ACTN Unreviewed; 642 AA.
AC A0A0F7CNV2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=2-oxoacid:acceptor oxidoreductase, alpha subunit {ECO:0000313|EMBL:AKG43556.1};
GN ORFNames=SXIM_21720 {ECO:0000313|EMBL:AKG43556.1};
OS Streptomyces xiamenensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=408015 {ECO:0000313|EMBL:AKG43556.1, ECO:0000313|Proteomes:UP000034034};
RN [1] {ECO:0000313|Proteomes:UP000034034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A01550 {ECO:0000313|Proteomes:UP000034034};
RA Xu J.;
RT "Complete genome sequence of a mangrove-derived Streptomyces xiamenensis.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP009922; AKG43556.1; -; Genomic_DNA.
DR RefSeq; WP_030736502.1; NZ_CP009922.3.
DR AlphaFoldDB; A0A0F7CNV2; -.
DR STRING; 408015.SXIM_21720; -.
DR KEGG; sxi:SXIM_21720; -.
DR PATRIC; fig|408015.6.peg.2204; -.
DR HOGENOM; CLU_017038_1_0_11; -.
DR Proteomes; UP000034034; Chromosome.
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}.
FT DOMAIN 38..225
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 280..491
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 68536 MW; 933D35FB8E3767D4 CRC64;
MTSQVDQVDP SGQERGSADA KEVKRLDRVI IRFAGDSGDG MQLTGDRFTS ETASFGNDLS
TLPNFPAEIR APAGTLPGVS SFQVHFADHD ILTPGDAPNV LVAMNPAALK ANIADVPRGA
EIIVNTDEFG GRAMLKVGYD SNPLEDGSLE GYSVHQVPLT TLTVEALKGF ELTRKEAGRS
KNMFALGLLS WMYHRPTEGT EAFLRAKFAK RPEIAEANIT AFRAGWNFGE TTEDFAVSYE
VAPATSAFPA GTYRNISGNL ALSYGLIAAA QQSELPLYLG SYPITPASDI LHELSRHKNF
GIRTFQAEDE IAGIGAALGA AFGGALGVTT TSGPGVALKA ETIGLAVSLE LPLLIVDIQR
GGPSTGLPTK TEQADLLQAM YGRNGEAPVP IVAPATPADC FTAALDAARI ALTYRTPVFL
LSDGYLANGS EPWRVPEVSE LPDLRVSFAT GPNHTLEDGN EVFWPYKRDP QTLARPWAIP
GTPGLEHRIG GIEKQDGTGN ISYSPSNHEF MVRTRQAKVD GIDVPLLEVD DPGADARTLV
LGWGSTYGPI TAAVRRIRRA GGTVAQAHLR NLNPFPANLG QVLAGYDRVV VPEMNLGQLA
SLLRARYLVD VESITQVTGL PFKAEQLANA IQDAERGPSD DH
//
