ID A0A1L3MS64_9BACI Unreviewed; 578 AA.
AC A0A1L3MS64;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:APH05179.1};
GN ORFNames=A9C19_10700 {ECO:0000313|EMBL:APH05179.1};
OS Bacillus weihaiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1547283 {ECO:0000313|EMBL:APH05179.1, ECO:0000313|Proteomes:UP000181936};
RN [1] {ECO:0000313|EMBL:APH05179.1, ECO:0000313|Proteomes:UP000181936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alg07 {ECO:0000313|EMBL:APH05179.1,
RC ECO:0000313|Proteomes:UP000181936};
RX PubMed=27901120; DOI=10.1038/srep38248;
RA Zhu Y., Chen P., Bao Y., Men Y., Zeng Y., Yang J., Sun J., Sun Y.;
RT "Complete genome sequence and transcriptomic analysis of a novel marine
RT strain Bacillus weihaiensis reveals the mechanism of brown algae
RT degradation.";
RL Sci. Rep. 6:38248-38248(2016).
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DR EMBL; CP016020; APH05179.1; -; Genomic_DNA.
DR RefSeq; WP_072579973.1; NZ_CP016020.1.
DR AlphaFoldDB; A0A1L3MS64; -.
DR STRING; 1547283.A9C19_10700; -.
DR KEGG; bwh:A9C19_10700; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000181936; Chromosome.
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:UP000181936}.
FT DOMAIN 14..175
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 210..449
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 476..570
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 578 AA; 63815 MW; A6064B4AD5E059AE CRC64;
MVNQLSWKVG GQQGEGIEST GEVFSIALNR LGYYLYGYRH FSSRIKGGHT NNKIRVSTTQ
VRSISDDLDI LVAFDQETID VNVHELKESG IVLADAKFNP TIPEGENVTL YSVPFTEIAT
ELGTSLMKNM VAIGASSAIL NINTEQFHDV VQDTYGKKGE KIVEKNMQAI EKGAEYLKKE
LGFNRQDMFL EKADGKKRMF MIGNDAIALG ALAGGSRFMA AYPITPASEI MEYLIKKLPK
FGGAVIQTED EIAACTMAIG ANYAGARTFT ASAGPGLSLM MEAIGLSGMT EQPLVIIDTQ
RGGPSTGLPT KQEQSDLMAM IYGTHGEIPK VVMAPSTVEE AFYDTIEAFN IAEEYQVPVI
LLTDLQLSLG KQTVDPLHYN KIEIRRGKLL SEELPERENK EYFKRFEVTE DGISPRVIPG
MKHGIHHVTG VEHDEAGKPS ESAVNRVAQM DKRLRKLNHL NFPNPIHKNI QHESPDVLLV
GFISTRGTIE EAMERLELDG VKVNHAQIRL IHPFPTEELL PLVEAAKKVI VVENNATGQL
ASLLKMNVGN AQKISSLLKY DGNPFLPQEI YTRSKELI
//
