(data stored in SCRATCH zone)

SWISSPROT: D5E9T0_METMS

ID   D5E9T0_METMS            Unreviewed;       447 AA.
AC   D5E9T0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 54.
DE   SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ADE35931.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Mmah_0399 {ECO:0000313|EMBL:ADE35931.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35931.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35931.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|RuleBase:RU003691}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001994; ADE35931.1; -; Genomic_DNA.
DR   RefSeq; WP_013036874.1; NC_014002.1.
DR   EnsemblBacteria; ADE35931; ADE35931; Mmah_0399.
DR   GeneID; 8982534; -.
DR   KEGG; mmh:Mmah_0399; -.
DR   eggNOG; arCOG01068; Archaea.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276712; -.
DR   KO; K00383; -.
DR   OMA; KCAIIEA; -.
DR   OrthoDB; 19112at2157; -.
DR   BioCyc; MMAH547558:G1GHT-396-MONOMER; -.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E9T0.
DR   SWISS-2DPAGE; D5E9T0.
KW   FAD {ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003691};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN          5..319
FT                   /note="Pyr_redox_2"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          339..444
FT                   /note="Pyr_redox_dim"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   447 AA;  48618 MW;  BC701A1C65AA041C CRC64;
     MAREYDIVII GTGVAGTVCA NKASAAGMKI AITDIREYGG TCALRGCVPK KVLVGVAETV
     EQVNRFNKLG IMPQSSVNWN KLMDFKQTFV DNFPQNKEEK FTNMDIDTYH GGAKFVSKNE
     VKIADTILKG KHILIAPGSV PRKTGIKGEE NLITSEQFLN LDELPRKIVF VGGGYISFEL
     AHIAARAGSQ VTILQRSEVL KQFDRDMVKL LVKASEEAGI NVNTGISVSS VESTSSGFTV
     NTRNREGKES RIECDLVVNG SGRIAALEGM ELEKGNVETK DGFVETNDYM QSVSNPYVYA
     AGDCVKPGAP LTPVASLQGT TAADNMIKGN VKTVDYTGIP STVFTLPPLS SVGISLSEST
     DRYEVLIHDR SHWYNSRRLS ENYAASKVII EKESQKIAGA HILGSHSEEV INIFAMAIRL
     GLTLSQFKKV VYVFPTVSSE IQSMIRG
//

If you have problems or comments...

PBIL Back to PBIL home page