ID D2BG54_DEHMV Unreviewed; 677 AA.
AC D2BG54;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Pyridine nucleotide-disulphide oxidoreductase protein {ECO:0000313|EMBL:ACZ61304.1};
GN OrderedLocusNames=DhcVS_131 {ECO:0000313|EMBL:ACZ61304.1};
OS Dehalococcoides mccartyi (strain VS).
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=311424 {ECO:0000313|EMBL:ACZ61304.1, ECO:0000313|Proteomes:UP000002506};
RN [1] {ECO:0000313|EMBL:ACZ61304.1, ECO:0000313|Proteomes:UP000002506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS {ECO:0000313|EMBL:ACZ61304.1,
RC ECO:0000313|Proteomes:UP000002506};
RX PubMed=19893622; DOI=10.1371/journal.pgen.1000714;
RA McMurdie P.J., Behrens S.F., Muller J.A., Goke J., Ritalahti K.M.,
RA Wagner R., Goltsman E., Lapidus A., Holmes S., Loffler F.E., Spormann A.M.;
RT "Localized plasticity in the streamlined genomes of vinyl chloride
RT respiring Dehalococcoides.";
RL PLoS Genet. 5:E1000714-E1000714(2009).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; CP001827; ACZ61304.1; -; Genomic_DNA.
DR AlphaFoldDB; D2BG54; -.
DR KEGG; dev:DhcVS_131; -.
DR eggNOG; COG0493; Bacteria.
DR eggNOG; COG1143; Bacteria.
DR eggNOG; COG1145; Bacteria.
DR HOGENOM; CLU_000422_3_4_0; -.
DR Proteomes; UP000002506; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.70.3270; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF00037; Fer4; 2.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002506};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 654..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 109..138
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 601..630
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 677 AA; 74098 MW; C7F14C5C5B46FFEC CRC64;
MILISYFCFV NPLFETLLSL HTDTGYRVGQ RTEGVVELTC LSRQRSSRID NVLYVASIIS
GTRSFKYRRK YFKKETYMAK TKAPVEKLES AEEIQKDGKV VSTKRTKGSE FFWTQSRCTG
CNRCASVCPV DAIKLDRDKT PTKRVGTSPC TRACPAGLDI PRYVRFVADG NASAATAVMR
EKIPFPSVCG YVCFHPCELE CQRQKFDEPI AIRALKRYAA ENDDGSWKNN LKIAPPTGKK
VAIIGSGPAG LTSAYFLTLL GHEATIFESM EYAGGKMFYS IPEHQLPKDI LNKEIKTITD
LGVTIHTSCQ VQSVQTLFKQ GYNSVLLSTG VLGLDEGLLL PCDETVESNL IKGSDFLKSI
KSTTKESLGD KVVVIGGGSE AYNSAFAAKN LGVSEVHLVC SRHTGSKEAS PEEVDRAIDA
GVTVHPSLDF VKLVKSDDKI EGVELFRIRS YGYDKDNRLH YEIINDTRCL IPADTVITTV
APDEKPGADY LTVVQPGVFA AGDGISGARS VIEAMAAGRS VAGLIDKYLG GEGNLDETLA
PPEKDIKPLS EPKGQNRSQI ELNLVKQAGG DKVEIEKTLS PEAAKKEARR CLRCDIVHQV
HDYSLDTSSC TYCGRCVNAC YWDAITSGYG YEAAAKKRQA EIAALEEKHS VYNYAIRILP
IAIGLMILAA AVAKLFK
//