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Database: UniProt/TrEMBL
Entry: C8XJA7_NAKMY
LinkDB: C8XJA7_NAKMY
Original site: C8XJA7_NAKMY 
ID   C8XJA7_NAKMY            Unreviewed;       469 AA.
AC   C8XJA7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   19-MAR-2014, entry version 31.
DE   SubName: Full=Pyridine nucleotide-disulphide oxidoreductase dimerisation region;
GN   OrderedLocusNames=Namu_2195;
OS   Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / JCM 9543 /
OS   Y-104) (Microsphaera multipartita).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Frankineae; Nakamurellaceae; Nakamurella.
OX   NCBI_TaxID=479431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700099 / DSM 44233 / JCM 9543 / Y-104;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Ovchinnikova G., Sims D., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Nakamurella multipartita DSM 44233.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; CP001737; ACV78572.1; -; Genomic_DNA.
DR   RefSeq; YP_003201561.1; NC_013235.1.
DR   ProteinModelPortal; C8XJA7; -.
DR   STRING; 479431.Namu_2195; -.
DR   EnsemblBacteria; ACV78572; ACV78572; Namu_2195.
DR   GeneID; 8447806; -.
DR   KEGG; nml:Namu_2195; -.
DR   PATRIC; 22661990; VBINakMul62011_2221.
DR   eggNOG; COG1249; -.
DR   HOGENOM; HOG000276709; -.
DR   KO; K17883; -.
DR   OMA; VKRVFGR; -.
DR   OrthoDB; EOG6QCD6D; -.
DR   BioCyc; NMUL479431:GHQL-2225-MONOMER; -.
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   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; FAD; Flavoprotein; Oxidoreductase;
KW   Redox-active center.
SQ   SEQUENCE   469 AA;  50762 MW;  89385F7523D7DD81 CRC64;
     MHFDLVVVGS GSGNTILGRE FRDQRVALVE SGAFGGTCLN AGCIPTKSFV YPADLADAVT
     RADRLGLKAT VAPVDWAVLR DRIFSRTDEI SAHGLEYRQG DKWPNLEMLT GIARFTGVKS
     MAVDLTAGGR VDLTADRFVL AAGGRPVIPD IPGLDEEIVG EGVVHTSDTI MRIAQRPDRI
     VIIGGGYIAA EFAHVFDAFG SRVTQVVRGS RLLRHHDEDV ATTFTDHVRA RYDLRRDTEI
     CGIKPLDGQG VRVFLEGPYG EATVDADVLL LATGRRPNSD LLNLPATGVT VNEQSRVVVD
     EYQETVVPGI YALGDLSSPY ALKHVANHEA RVVRHNLNHP DDRITTDHRF VPAAVFTEPQ
     IAAVGLTEQQ AREQGVEYVV GRRDYGGTAA GWAREDTTGF AKVLADPRTG LLLGAHVIGP
     EAATVIQPLV QAMSFGQRAH DVARGQYWIH PALPEVIENA LLALPRPTG
//
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