ID A0A074M6Q6_9BACL Unreviewed; 576 AA.
AC A0A074M6Q6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:KEO81667.1};
GN ORFNames=EL26_19545 {ECO:0000313|EMBL:KEO81667.1};
OS Tumebacillus flagellatus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Tumebacillus.
OX NCBI_TaxID=1157490 {ECO:0000313|EMBL:KEO81667.1, ECO:0000313|Proteomes:UP000027931};
RN [1] {ECO:0000313|EMBL:KEO81667.1, ECO:0000313|Proteomes:UP000027931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GST4 {ECO:0000313|EMBL:KEO81667.1,
RC ECO:0000313|Proteomes:UP000027931};
RX PubMed=23435245; DOI=10.1099/ijs.0.045351-0;
RA Wang Q., Xie N., Qin Y., Shen N., Zhu J., Mi H., Huang R.;
RT "Tumebacillus flagellatus sp. nov., an alpha-amylase/pullulanase-producing
RT bacterium isolated from cassava wastewater.";
RL Int. J. Syst. Evol. Microbiol. 63:3138-3142(2013).
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:KEO81667.1}.
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DR EMBL; JMIR01000033; KEO81667.1; -; Genomic_DNA.
DR RefSeq; WP_038092499.1; NZ_JMIR01000033.1.
DR AlphaFoldDB; A0A074M6Q6; -.
DR STRING; 1157490.EL26_19545; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000027931; 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:UP000027931}.
FT DOMAIN 14..175
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 209..450
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 475..538
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 576 AA; 63062 MW; AB9EA61DB461023E CRC64;
MLEQLSWKVG GQQGEGIDST GNILATSLNR HGYFIYGYRH FSSRIKGGHT NYKIRISTKS
RLANADYLDI LIAFDQETID FNSHELRENG VLIADAKFNP VAPEGKQIRF FAVPLTKIAE
ENGSAIMKNM VAVGATAAVL GLSPETFLSY LNDKFLRKGE QVVQNNMNAL KAGFQYVIDQ
GIELSDLKLA PGDGVERLYL TGNDACGFGA LAAGVRLMPA YPITPASEIM EYLIKKLPKV
GGHVLQTEDE IAAVTMSIGA SFGGSRVCTS TSGPGLALMM EGIGLAGITE TPIVIFDTQR
GGPSTGMPTK HEQSDMYAAL WGTHGEIQKI VVAPSNAEEC FYMTVDAFNW AEQYQVPTII
LTDLALSMSD QTVEKFDFSR VSIDRGNLAT QEQLEAVAAG QLFKRYEFTD SKISPRVFPG
QKGGIHHVTG VEHTEVGRPT EDKNIRNKMM DKRLGKFDGI ELPNSFSFNG DEDFDTLLIG
VGSTAGLIDE AMERLQAEGQ KVGHLHIKVL NPFPTESVQK FVSKAKKVVV IENNATGQLK
NIMRFNGVQG EFISQVKYDG NPYIPSEIFT FVKELN
//
