ID A0A0E9LZF6_9BACT Unreviewed; 447 AA.
AC A0A0E9LZF6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=2-oxoglutarate oxidoreductase, alpha subunit {ECO:0000313|EMBL:GAO30942.1};
GN ORFNames=JCM15548_13264 {ECO:0000313|EMBL:GAO30942.1};
OS Geofilum rubicundum JCM 15548.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Geofilum.
OX NCBI_TaxID=1236989 {ECO:0000313|EMBL:GAO30942.1, ECO:0000313|Proteomes:UP000032900};
RN [1] {ECO:0000313|EMBL:GAO30942.1, ECO:0000313|Proteomes:UP000032900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15548 {ECO:0000313|EMBL:GAO30942.1};
RX PubMed=25736980;
RA Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA Hattori M., Ohkuma M.;
RT "Distribution and evolution of nitrogen fixation genes in the phylum
RT bacteroidetes.";
RL Microbes Environ. 30:44-50(2015).
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:GAO30942.1}.
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DR EMBL; BAZW01000034; GAO30942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E9LZF6; -.
DR STRING; 1236989.JCM15548_13264; -.
DR Proteomes; UP000032900; 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; 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; 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.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000032900}.
FT DOMAIN 22..210
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 260..407
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 447 AA; 47930 MW; 426AF70F902603DA CRC64;
MGKSSKVIEV DKISVRFSGD SGDGMQLTGN LFSQTSAVYG NDISTFPDYP ADIRAPQGTI
GGVSGFQVNF GQGVTTPGDL TDVLVAMNPA ALKANAVFMK PGGTIIIDVD SFEAKGLEKA
GYQTDDPVFE DKLEGFNIIK APISSLTRES VKDLALDNKS VLRSKNMFAL GLVFWLFDRP
IEHTQAFIKN KFGSKPLIME ANLKVLQAGH DYGYTIQAVT PSYHINPTES RKGIYRNLNG
NKAAAWGFLL AAEKSGLSLF LGSYPITPAT EILQELAARK DLGVKVFQAE DEIAGVCTAI
GASFSGALGI TSTSGPGLAL KTEAIGLAVM SELPLVVVNV QRGGPSTGLP TKTEQADLLQ
ALFGRNGESP VVVMAASTPV NCFDYAFYAS KIAIEHMTPV ILLTDAFWPM VRNNGGFLMM
MSFRLSLSRP HTRSRVNFSL ICAMKND
//
