ID C8XJA7_NAKMY Unreviewed; 469 AA.
AC C8XJA7;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 01-MAY-2013, entry version 28.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; K00383; -.
DR OMA; PNSDLLN; -.
DR BioCyc; NMUL479431:GHQL-2225-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; 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 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; FAD/NAD-linked_reductase_dimer; 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
//