ID A0A0F7GDJ4_9CHLR Unreviewed; 306 AA.
AC A0A0F7GDJ4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Pyruvate:ferredoxin oxidoreductase beta subunit {ECO:0000313|EMBL:AKG53687.1};
DE EC=1.2.7.1 {ECO:0000313|EMBL:AKG53687.1};
GN ORFNames=DGWBC_1028 {ECO:0000313|EMBL:AKG53687.1};
OS Dehalogenimonas sp. WBC-2.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=943347 {ECO:0000313|EMBL:AKG53687.1, ECO:0000313|Proteomes:UP000034106};
RN [1] {ECO:0000313|EMBL:AKG53687.1, ECO:0000313|Proteomes:UP000034106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WBC-2 {ECO:0000313|EMBL:AKG53687.1,
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; AKG53687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7GDJ4; -.
DR STRING; 943347.DGWBC_1028; -.
DR KEGG; dew:DGWBC_1028; -.
DR PATRIC; fig|943347.4.peg.1068; -.
DR Proteomes; UP000034106; Chromosome.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd03376; TPP_PFOR_porB_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR42897; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR PANTHER; PTHR42897:SF2; PYRUVATE SYNTHASE SUBUNIT PORB; 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,
KW ECO:0000313|EMBL:AKG53687.1}; Pyruvate {ECO:0000313|EMBL:AKG53687.1}.
FT DOMAIN 51..219
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 306 AA; 33554 MW; 450EF0A420856876 CRC64;
MQNLGIYASR LVTKEENFVP GHRACIGCGE ALAVRLAAKA FGHNTIVVNA TGCMEIVASQ
LPYTSWKLPW IHTLFENSAA VASGVEAGLR AQMRKGKLPQ EDINVVAIAG DGATFDIGLQ
ALSGAMERGH NFTYLCFDNE AYMNTGIQRS SATPFGASTT TSPAGKVQAG QSSWKKNMPE
IAVAHNIPYV ATACPSYPFD LIEKVKKGLA VKGPAYIHIM SVCPTGWRCD TEITIMLGRL
AVETGIFPLY EVENGKYKMS LVPEKLKPID DYMKLQRRFR HIKPDVLQQI QTRVVAEYEK
LLEKAV
//