ID A0A3A9KA42_9BACI Unreviewed; 580 AA.
AC A0A3A9KA42;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:RKL69069.1};
GN ORFNames=CR203_03235 {ECO:0000313|EMBL:RKL69069.1};
OS Salipaludibacillus neizhouensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=885475 {ECO:0000313|EMBL:RKL69069.1, ECO:0000313|Proteomes:UP000281498};
RN [1] {ECO:0000313|EMBL:RKL69069.1, ECO:0000313|Proteomes:UP000281498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 13187 {ECO:0000313|EMBL:RKL69069.1,
RC ECO:0000313|Proteomes:UP000281498};
RA Wang H.;
RT "Bacillus sp. nov., a halophilic bacterium isolated from a Keqin Lake.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:RKL69069.1}.
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DR EMBL; PDOE01000001; RKL69069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9KA42; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000281498; 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; 3.40.50.920; -; 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; IPR033412; PFOR_II.
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; PF17147; PFOR_II; 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:UP000281498}.
FT DOMAIN 14..175
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 210..452
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 478..570
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 580 AA; 63390 MW; 1124235C8FF7AA9D CRC64;
MINQLSWKVG GQQGEGIEST GEIFSMALNR QGYFLYGYRH FSSRIKGGHT NNKIRVSIKA
TNSISDDLDI LVAFDQETID VNHHELSLGA VVIGDSKFTP SLPEGSHAKL FSVPFTKIAT
DLGTSLMKNM VAVGASAAVI GLNPEMFKSV VEQIFSKKGA TVVEKNMDAI RAGMEYFQKE
ASGNVGDFSL EKADGKHRMF MIGNDAIALG ALTGGARFMP AYPITPASEI MEYLIRKLPD
YGGTVIQTED EIAACTMAIG ANYAGVRSLT ASAGPGLSLM MEGIGLSGMT ETPLVIIDTQ
RGGPSTGLPT KQEQSDIFAV IFGTHGEIPK VVLAPSSVEE AFYDTIEAFN IAEEYQVPVI
LMTDLALSLG KQTVEPLDFE KVEIRRGKLD PEEVLPEQEK GVYFKRYDVT EDGISKRVIP
GMPNGLHHVT GVEHNEQGKP SESPENRKAQ MDKRMRKLDT LIANFPVPVV KDEKHDNADV
LILGVNSTRG TIQEAIPMLE KDGVKVNHGQ IRLLHPFPTD ELESMIDKAK KVIVIENNAT
GQVAQLLKMN TRLNKVESIL KYDGNPFLPS EIHNRCKEVL
//
