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Database: UniProt
Entry: A0A1A2N8N5_9MYCO
LinkDB: A0A1A2N8N5_9MYCO
Original site: A0A1A2N8N5_9MYCO 
ID   A0A1A2N8N5_9MYCO        Unreviewed;       282 AA.
AC   A0A1A2N8N5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=NAD-dependent protein deacetylase {ECO:0000256|HAMAP-Rule:MF_01967};
DE            EC=2.3.1.286 {ECO:0000256|HAMAP-Rule:MF_01967};
DE   AltName: Full=Regulatory protein SIR2 homolog {ECO:0000256|HAMAP-Rule:MF_01967};
GN   Name=cobB {ECO:0000256|HAMAP-Rule:MF_01967};
GN   ORFNames=A5695_18990 {ECO:0000313|EMBL:OBH11492.1};
OS   Mycobacterium sp. E1747.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834128 {ECO:0000313|EMBL:OBH11492.1, ECO:0000313|Proteomes:UP000092218};
RN   [1] {ECO:0000313|Proteomes:UP000092218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E1747 {ECO:0000313|Proteomes:UP000092218};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Sam S., Sreng N.,
RA   Him V., Kerleguer A., Cheng S.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NAD-dependent protein deacetylase which modulates the
CC       activities of several enzymes which are inactive in their acetylated
CC       form. {ECO:0000256|HAMAP-Rule:MF_01967}.
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:0000256|HAMAP-Rule:MF_01967};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01967};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01967};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01967}.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class II subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01967}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBH11492.1}.
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DR   EMBL; LZJI01000072; OBH11492.1; -; Genomic_DNA.
DR   RefSeq; WP_068079588.1; NZ_LZJI01000072.1.
DR   AlphaFoldDB; A0A1A2N8N5; -.
DR   STRING; 1834128.A5695_18990; -.
DR   OrthoDB; 9800582at2; -.
DR   Proteomes; UP000092218; Unassembled WGS sequence.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01409; SIRT4; 1.
DR   Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   HAMAP; MF_01967; Sirtuin_ClassII; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR003000; Sirtuin.
DR   InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR   InterPro; IPR026587; Sirtuin_class_II.
DR   InterPro; IPR026590; Ssirtuin_cat_dom.
DR   PANTHER; PTHR47651; NAD-DEPENDENT HISTONE DEACETYLASE HST4; 1.
DR   PANTHER; PTHR47651:SF7; NAD-DEPENDENT PROTEIN DEACYLASE SIR-2.2; 1.
DR   Pfam; PF02146; SIR2; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   PROSITE; PS50305; SIRTUIN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01967};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01967};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01967};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01967};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01967}.
FT   DOMAIN          1..279
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   ACT_SITE        119
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01967,
FT                   ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         25..45
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01967"
FT   BINDING         101..104
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01967"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01967,
FT                   ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01967,
FT                   ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01967,
FT                   ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01967,
FT                   ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         221..223
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01967"
FT   BINDING         247..249
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01967"
FT   BINDING         265
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01967"
SQ   SEQUENCE   282 AA;  29744 MW;  3B995B9D01FA2715 CRC64;
     MTTRCAESPE LVALLAGRRI AVLTGAGLST DSGIPDYRGP DSPPSNPMTI RQFTSDPAFR
     QRYWARNHIG WRHMDDTLPN AGHRALAALE RASVVTGLIT QNVDLLHTKA GSANVVNLHG
     TYARVVCLGC GYTMSRAALA DQLEALNPGF IERAEAVGGL AVAPDADAVV ADTASFRYLD
     CPSCGGMLKP DIVYFGESVT KAVVDQAYSL VDEADALLVA GSSLTVFSGY RFARHAAALG
     TPIAIINRGP TRGDDLASVK VDGGCSELLT LLVDELSPLA ML
//
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