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Database: UniProt
Entry: A0A0S8EGC0_9CHLR
LinkDB: A0A0S8EGC0_9CHLR
Original site: A0A0S8EGC0_9CHLR 
ID   A0A0S8EGC0_9CHLR        Unreviewed;       296 AA.
AC   A0A0S8EGC0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=2-oxoacid ferredoxin oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMJ77_06065 {ECO:0000313|EMBL:KPK46427.1};
OS   Dehalococcoidia bacterium SM23_28_2.
OC   Bacteria; Chloroflexota; Dehalococcoidia.
OX   NCBI_TaxID=1703396 {ECO:0000313|EMBL:KPK46427.1, ECO:0000313|Proteomes:UP000054036};
RN   [1] {ECO:0000313|EMBL:KPK46427.1, ECO:0000313|Proteomes:UP000054036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_28_2 {ECO:0000313|EMBL:KPK46427.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KPK46427.1}.
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DR   EMBL; LJUA01000074; KPK46427.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8EGC0; -.
DR   STRING; 1703396.AMJ77_06065; -.
DR   PATRIC; fig|1703396.3.peg.774; -.
DR   Proteomes; UP000054036; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03375; TPP_OGFOR; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR011896; OFOB.
DR   InterPro; IPR032686; PFO_beta_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR02177; PorB_KorB; 1.
DR   PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR   PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   Pfam; PF12367; PFO_beta_C; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          57..198
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   DOMAIN          202..268
FT                   /note="Pyruvate ferredoxin oxidoreductase beta subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12367"
SQ   SEQUENCE   296 AA;  32296 MW;  CE91295A7690DF29 CRC64;
     MITRLDPKVY DTAVEVTWCA GCGDYAILKA LKLALADMEI APHQVLLVSG IGCGSKLPDY
     MNANGYMTIH GRPLAVATGA KLANPDLHVI VVNGDGDSYG IGGNHFLHTC RRNPNITQIV
     ENNQIYGLTK GQYSPTSDAG FITTTSPDGA FEAALNPAAV ALAAGATFIA RSFSGDPKHL
     AEVIAQGVRH RGYALIDVLQ PCVTFNRVNT YAWYRERVYH LEEEQGYDHS DRAAAWHKAQ
     EWGERIPVGV IYQVDGVPPY EEQVRALEDG SPVSRLLELA RAPALEQYEG LKEQFV
//
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