(data stored in SCRATCH zone)

SWISSPROT: D6ZA88_SEGRD

ID   D6ZA88_SEGRD            Unreviewed;       473 AA.
AC   D6ZA88;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 52.
DE   SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ADG96630.1};
GN   OrderedLocusNames=Srot_0141 {ECO:0000313|EMBL:ADG96630.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96630.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96630.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
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DR   EMBL; CP001958; ADG96630.1; -; Genomic_DNA.
DR   STRING; 640132.Srot_0141; -.
DR   EnsemblBacteria; ADG96630; ADG96630; Srot_0141.
DR   KEGG; srt:Srot_0141; -.
DR   eggNOG; ENOG4105DX1; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276708; -.
DR   KO; K00322; -.
DR   OMA; VIPWTTF; -.
DR   Proteomes; UP000002247; 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: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   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.
PE   4: Predicted;
DR   PRODOM; D6ZA88.
DR   SWISS-2DPAGE; D6ZA88.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW   NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247}.
FT   DOMAIN        9    330       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      350    457       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
FT   NP_BIND     187    194       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING      56     56       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     210    210       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     274    274       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     315    315       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
SQ   SEQUENCE   473 AA;  50999 MW;  69E0844ED140A32D CRC64;
     MSSSASPRYD LVVIGSGPGG QKAAIAAAKL GKSVAIVERK HMLGGVCLNT GTIPSKTLRE
     AVLYLTGMNQ RELYGASYRV KSNITPEDLF ARTAQVIGKE TEVVRSQLQR NRVEIFPGVA
     SFVDEHTVEV VDDDRGESTR LHGEFFVIAT GTRPARLPGV NYDEERILDS DEILQLKAIP
     ATMVVVGAGV IGIEYASMFA ALGTRVTVVE RRPSMLEFCD PEVIEALRFH LRDLAVTFRF
     GEEVTDIEVG PNGAVTKLAS GKRIPAETVM YSAGRQGQTE ALALENAGLS ADDRGRIQVD
     KHFQTAVDHI YAVGDVIGFP ALAATSMDQG RLAAYHAFGE SAEGMTELQP IGIYSIPEVS
     YVGATETELT KAAVPYEVGV SRYRELARGQ IAGDSYGMLK LLVNTDDRKL LGVHIFGSQA
     TELVHIGQAV MGCGGTVDYL IEAVFNYPTL SEAYKVAALD VANKIRALAQ YCD
//

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