ID A0A0F7CU23_9CHLR Unreviewed; 574 AA.
AC A0A0F7CU23;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=2oxoglutarate oxidoreductase alpha subunit {ECO:0000313|EMBL:AKG53925.1};
DE EC=1.2.7.3 {ECO:0000313|EMBL:AKG53925.1};
GN ORFNames=DGWBC_1276 {ECO:0000313|EMBL:AKG53925.1};
OS Dehalogenimonas sp. WBC-2.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=943347 {ECO:0000313|EMBL:AKG53925.1, ECO:0000313|Proteomes:UP000034106};
RN [1] {ECO:0000313|EMBL:AKG53925.1, ECO:0000313|Proteomes:UP000034106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WBC-2 {ECO:0000313|EMBL:AKG53925.1,
RC ECO:0000313|Proteomes:UP000034106};
RX PubMed=26452554; DOI=10.1128/AEM.02017-15;
RA Molenda O., Quaile A.T., Edwards E.A.;
RT "Dehalogenimonas sp. Strain WBC-2 Genome and Identification of Its trans-
RT Dichloroethene Reductive Dehalogenase, TdrA.";
RL Appl. Environ. Microbiol. 82:40-50(2015).
RN [2] {ECO:0000313|Proteomes:UP000034106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WBC-2 {ECO:0000313|Proteomes:UP000034106};
RA Molenda O., Edwards E.A.;
RT "Identification of trans-1,2-dichloroethene reductive dehalogenase (TdrA)
RT in Dehalogenimonas sp. WBC-2.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP011392; AKG53925.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7CU23; -.
DR STRING; 943347.DGWBC_1276; -.
DR KEGG; dew:DGWBC_1276; -.
DR PATRIC; fig|943347.4.peg.1318; -.
DR Proteomes; UP000034106; Chromosome.
DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:AKG53925.1}.
FT DOMAIN 13..174
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 209..447
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 471..545
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 574 AA; 61640 MW; FC4E7233986FACC4 CRC64;
MPLDFNILIG GEAGQGVQSV GSVLAKTLMR GGYEVFADQD FESRIRGGHS FTRVRVSDCP
VESPSEKVDM LLSLNGETTE KHLSDMRRGG IIISDEEKTG AANAGKILFL DIPISKIAQE
TTGNLRMTNT VASAAALGLL DYDFEVLAGV LRQEYGRHGE QVAADNIKAA RAGFNFAQTN
CPKGYKKRLK AGKSSGKMLV SGNEAVALGA IAAGCQFVSG YPMTPSTPIL EFLADKGRDF
RIPVIQAEDE IAAINMAVGA AYTGARSLVA TSGGGFCLMT EGLSLAGMTE TPVVIILGQR
AGPSTGLPTR TEQGELEFAL HAGHGEFPRI IMAPANATEA FWLTIKAFNL AEKYQSPAII
LTDHEMADSY YTVSPFDLGA IAIERGVLTD QEAEKQIDYK RYAYTESGIS PRAFPGQGKA
LVVADSDEHS EAGHIIEDAE TRRLMVEKRM RKQEGIKQEI GAPAIIHRDD AKYNLIGWGS
SRGAIEEAAM LLEAKGINVC VIHLAELWPF PAEAIIEALA GVADNIVVES NATGQLGRLI
RTETGIKADA HITRYDGRPL SAEYIIENFA WKAA
//
