ID D2Z6K9_9BACT Unreviewed; 560 AA.
AC D2Z6K9;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:EFC91106.1};
GN ORFNames=Dpep_1080 {ECO:0000313|EMBL:EFC91106.1};
OS Dethiosulfovibrio peptidovorans DSM 11002.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Dethiosulfovibrio.
OX NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC91106.1, ECO:0000313|Proteomes:UP000006427};
RN [1] {ECO:0000313|EMBL:EFC91106.1, ECO:0000313|Proteomes:UP000006427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC91106.1,
RC ECO:0000313|Proteomes:UP000006427};
RX PubMed=21304695;
RA Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T., Nolan M.,
RA Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Goodwin L., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans type
RT strain (SEBR 4207).";
RL Stand. Genomic Sci. 3:85-92(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:EFC91106.1}.
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DR EMBL; ABTR02000001; EFC91106.1; -; Genomic_DNA.
DR RefSeq; WP_005660294.1; NZ_ABTR02000001.1.
DR AlphaFoldDB; D2Z6K9; -.
DR STRING; 469381.Dpep_1080; -.
DR PaxDb; 469381-Dpep_1080; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000006427; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00158; RHOD; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006427}.
FT DOMAIN 475..558
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 560 AA; 60949 MW; E9FDBA0B5FB5EF3B CRC64;
MSKKIVVIGG VACGGKTAAR LRRLDPEAEI LILEKGPYLS YAGCGLPYYI EGIVKEYKEL
MCTPVGVVRD ESYFLNVKKI DVLTRHMATC IDREKKEVVA VDLELAVEKR FPYDDLVIAT
GGSPIKPDLP GIELGTVFTL WTLSDALAMR AAIDNGNVKR AVVVGAGLIG MEVVEALVAR
DIEVSVVDLL SWPLPNMLDE EFGSRLLREL KAKGVHFYGN EKVLEILGQD SVLTGVKTDQ
RTIPADMVLL AIGVRPNIHL AEETGLDIGS SGGVAVDEYM RTSDPNIYAG GDCVEVRHIL
TGKGVRQPMG SSANREGRVI ADNILGRGST FKGVLGTAIM KFFEYTVGRT GFNEHQARKE
GFDPISVTVT APDKPHFMPG AAWMVIKLVA DKNTKRLLGG QIFGPGAVDK RLDGLVTAVT
GGLTVDDLAD TDFAYAPPYA TALDPMTQTA NVLRNKMEGL MTSYSPRELA AKMDRGEDCV
LLDVRTEGEI KLQGKLPYEN QVHIPLGALW TRVEELPKDK EIIAFCKISL RGWDALTVLR
SKGFHKVAIL EGGMMGWPYG
//
