(data stored in ACNUC7421 zone)

HOGENOM: NEMEN2_1_PE10

ID   NEMEN2_1_PE10                        STANDARD;      PRT;   753 AA.
AC   NEMEN2_1_PE10; A1INN2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=NADH-quinone oxidoreductase; EC=1.6.99 5; (NEMEN2_1.PE10).
GN   OrderedLocusNames=NMA0010;
OS   NEISSERIA MENINGITIDIS Z2491.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS NEMEN2_1.PE10.
CC       Neisseria meningitidis Z2491, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:A1INN2_NEIMA
CC   -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC   -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC   -!- GENE_FAMILY: HOG000031442 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A1INN2; -.
DR   EMBL; AL157959; CAM07339.1; -; Genomic_DNA.
DR   PIR; F81991; F81991.
DR   RefSeq; YP_002341573.1; NC_003116.1.
DR   ProteinModelPortal; A1INN2; -.
DR   EnsemblBacteria; EBNEIT00000000195; EBNEIP00000000195; EBNEIG00000000195.
DR   GeneID; 906028; -.
DR   GenomeReviews; AL157959_GR; NMA0010.
DR   KEGG; nma:NMA0010; -.
DR   GeneTree; EBGT00050000021481; -.
DR   OMA; CRQCLVD; -.
DR   ProtClustDB; PRK09129; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   InterPro; IPR009010; Asp_de-COase-like_fold.
DR   InterPro; IPR012675; Beta-grasp_ferredoxin-type.
DR   InterPro; IPR001041; Ferredoxin.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR   InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR   InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR   Gene3D; G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.
DR   Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR   SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR   SUPFAM; SSF50692; Asp_decarb_fold; 1.
DR   SUPFAM; SSF54292; Ferredoxin; 1.
DR   TIGRFAMs; TIGR01973; NuoG; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR   PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR   PROSITE; PS00643; COMPLEX1_75K_3; 1.
DR   HOGENOMDNA; NEMEN2_1.PE10; -.
KW   4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; NAD;
KW   Oxidoreductase.
SQ   SEQUENCE   753 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLQIEIDGKQ VSVEQGATVI EAAHKLGTYI PHFCYHKKLS IAANCRMCLV DVEKAPKPLP
     ACATPVTDGM IVRTHSAKAR EAQEGVMEFL LINHPLDCPT CDQGGECQLQ DLAVGYGKTT
     SRYTEEKRSV VGKDMGPLVS AEEMSRCIHC TRCVRFTEEI AGLQEIAMVN RGEHSEIMPF
     IGKTVETELS GNVIDLCPVG ALTSKPFRFN ARTWELNRRK SVSAHDALGS NLIVQTKDHT
     VRRVLPLENE AINECWLSDR DRFAYEGLYH ESRLKNPKIK QGGEWMDVDW KTALEYVRSA
     IECIAKDGNQ NQVGIWANPM NTVEELYLAK KLADGLGVKN FATRLRQQDK RLSDGIKGAQ
     WLGQSIESLA DNDAVLVVGA NLRKEQPLLT ARLRRAAKDR MALSVLAGSK EELFMPLLSQ
     EAAHPDEWAG RLKNLSANAE HAVTASLKNA EKAAVILGAE VQNHPDYAAI YAAVQELADA
     TGAVLGILPQ AANSVGADVL GVNSGESVAE MANAPKQAVL LLNVEPEIDT VDGAKAVAAL
     KQAKSVMAFT PFVSETLLDV CDVLLPIAPF TETSGSFINM EGRLQSFHGV VQGFGDSRPM
     WKVLRVLGNL FDLKGFEYHD TVAILKDALD AESLPSKLNN RAASTQKDFQ TASSRLVRVG
     GVGIYHTDAI VRRSAPLQET SHAAVPAARV NPNTLARLGL QDGQTAVAKQ NGASVSVAVK
     ADAGLPENVV HLPLHTENAA LGALMDTIEL AGA
//

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