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NPD_AERPE
ID   NPD_AERPE               Reviewed;         245 AA.
AC   Q9YB13;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=NAD-dependent protein deacylase {ECO:0000255|HAMAP-Rule:MF_01121};
DE            EC=2.3.1.286 {ECO:0000255|HAMAP-Rule:MF_01121};
DE   AltName: Full=Regulatory protein SIR2 homolog {ECO:0000255|HAMAP-Rule:MF_01121};
GN   Name=cobB {ECO:0000255|HAMAP-Rule:MF_01121}; OrderedLocusNames=APE_1782.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
CC   -!- FUNCTION: NAD-dependent lysine deacetylase and desuccinylase that
CC       specifically removes acetyl and succinyl groups on target proteins.
CC       Modulates the activities of several proteins which are inactive in
CC       their acylated form. Deacetylates the N-terminal lysine residue of
CC       Alba, the major archaeal chromatin protein and that, in turn, increases
CC       Alba's DNA binding affinity, thereby repressing transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01121}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-
CC         ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC         Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
CC         EC=2.3.1.286; Evidence={ECO:0000255|HAMAP-Rule:MF_01121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC         succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC         Xref=Rhea:RHEA:47668, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:87830, ChEBI:CHEBI:87832;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01121};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01121};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01121};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01121}.
CC   -!- DOMAIN: 2 residues (Tyr-66 and Arg-69) present in a large hydrophobic
CC       pocket are probably involved in substrate specificity. They are
CC       important for desuccinylation activity, but dispensable for
CC       deacetylation activity. {ECO:0000255|HAMAP-Rule:MF_01121}.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class III subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01121}.
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DR   EMBL; BA000002; BAA80785.2; -; Genomic_DNA.
DR   PIR; D72562; D72562.
DR   AlphaFoldDB; Q9YB13; -.
DR   SMR; Q9YB13; -.
DR   STRING; 272557.APE_1782.1; -.
DR   PRIDE; Q9YB13; -.
DR   EnsemblBacteria; BAA80785; BAA80785; APE_1782.1.
DR   KEGG; ape:APE_1782.1; -.
DR   PATRIC; fig|272557.25.peg.1194; -.
DR   eggNOG; arCOG04248; Archaea.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0036054; F:protein-malonyllysine demalonylase activity; IEA:InterPro.
DR   GO; GO:0036055; F:protein-succinyllysine desuccinylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006476; P:protein deacetylation; IEA:UniProtKB-UniRule.
DR   CDD; cd01412; SIRT5_Af1_CobB; 1.
DR   Gene3D; 3.30.1600.10; -; 1.
DR   HAMAP; MF_01121; Sirtuin_ClassIII; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR003000; Sirtuin.
DR   InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR   InterPro; IPR027546; Sirtuin_class_III.
DR   InterPro; IPR026590; Ssirtuin_cat_dom.
DR   Pfam; PF02146; SIR2; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   PROSITE; PS50305; SIRTUIN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; NAD; Reference proteome; Transcription;
KW   Transcription regulation; Transferase; Zinc.
FT   CHAIN           1..245
FT                   /note="NAD-dependent protein deacylase"
FT                   /id="PRO_0000110376"
FT   DOMAIN          5..245
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   ACT_SITE        118
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         22..41
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         100..103
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         149
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         186..188
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         212..214
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         241
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
SQ   SEQUENCE   245 AA;  27096 MW;  ED1DEDCE38BDEFA1 CRC64;
     MEAVWESARI LANSRFAVAF TGAGISAESG IPTFRGKDGL WSRFDPRDLA TPEAFNRDPR
     LVWEWYSWRI ERVLAAKPNK AHRLLARLED SGVLKAVITQ NVDGLHRRAG SRRVLELHGN
     VLRARCTRCG SKLEWREKPS NLPPSCPRCG GVLRPDVVWF GEPLDTSLLE EAFGLARRSD
     VMIIIGTSGA VDPAGLLPLA AKESGATLIN VNPEPNRYSG VADIELRMRA VEFAERLSRA
     MGIDI
 
 
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