ID N0AQX4_9BACI Unreviewed; 578 AA.
AC N0AQX4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:AGK53128.1};
GN ORFNames=B1NLA3E_06820 {ECO:0000313|EMBL:AGK53128.1};
OS Bacillus sp. 1NLA3E.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK53128.1, ECO:0000313|Proteomes:UP000013300};
RN [1] {ECO:0000313|EMBL:AGK53128.1, ECO:0000313|Proteomes:UP000013300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLA3E {ECO:0000313|EMBL:AGK53128.1};
RX PubMed=23833140;
RA Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA Brooks S., Kostka J.E., Green S.J.;
RT "Genome sequences for three denitrifying bacterial strains isolated from a
RT uranium- and nitrate-contaminated subsurface environment.";
RL Genome Announc. 1:e00449-13(2013).
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DR EMBL; CP005586; AGK53128.1; -; Genomic_DNA.
DR RefSeq; WP_015593188.1; NC_021171.1.
DR AlphaFoldDB; N0AQX4; -.
DR STRING; 666686.B1NLA3E_06820; -.
DR KEGG; baci:B1NLA3E_06820; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR HOGENOM; CLU_017038_1_0_9; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000013300; 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:UP000013300}.
FT DOMAIN 14..175
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 210..450
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 475..569
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 578 AA; 63484 MW; DA7632A97BD47348 CRC64;
MINQLSWKVG GQQGEGIEST GEIFSIALNR LGYYLYGYRH FSSRIKGGHT NNKIRVSTKQ
VRSISDDLDI LVAFDQETIE LNYKELHEHG VIIADTRFDP QQPADSKAPM YAVPFTEIAT
ELGTSLMKNM VAIGATSAVL DLDIQVFEEV VNEIFGKKGQ QVVAKNMEAI RAGFDYMKEK
IGDKIETMEL EKADGKKRLF MIGNDAIAMG AVAGGCRFMA AYPITPASEI MEYLIKHLPP
LGGAVIQTED EIAAATMAIG ANYGGVRAIT ASAGPGLSLK MEAIGLSGIT ETPLVIVDTQ
RGGPSTGLPT KQEQSDLMAM IYGTHGEIPK IVMAPSTVQE AFYDAAEAFN LAEEYQCPVI
LLTDLQLSLG KQTVEPLEFD KIEIRRGKLV QSELPEIENK GYFKRYEVTE DGVSPRSIPG
IKNGIHHVTG VEHAETGKPS ESAANRNAQM DKRFRKLENL KFNTPVYKNA PHEEADLLIV
GFNSTRGAIE EALIRLEQDG LKVNHAQIRL IHPFPVDEML PLVKSAKKIA VIENNATGQL
ANIIKMNVGC GEKVVKILKY DGNPFLPHEV YSKCKELF
//
