ID   A0A1S3KKA9_SALSA        Unreviewed;       186 AA.
AC   A0A1S3KKA9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=NAD-dependent protein deacylase sirtuin-5, mitochondrial-like {ECO:0000313|RefSeq:XP_013978769.1};
GN   Name=LOC106560408 {ECO:0000313|RefSeq:XP_013978769.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013978769.1};
RN   [1] {ECO:0000313|RefSeq:XP_013978769.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013978769.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_013978769.1; XM_014123294.1.
DR   AlphaFoldDB; A0A1S3KKA9; -.
DR   STRING; 8030.ENSSSAP00000044149; -.
DR   GeneID; 106560408; -.
DR   KEGG; sasa:106560408; -.
DR   OrthoDB; 4233219at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa10.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR003000; Sirtuin.
DR   InterPro; IPR026590; Ssirtuin_cat_dom.
DR   PANTHER; PTHR11085:SF12; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02146; SIR2; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   PROSITE; PS50305; SIRTUIN; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT   DOMAIN          1..186
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   ACT_SITE        79
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ   SEQUENCE   186 AA;  20227 MW;  4552A6F63D56B67A CRC64;
     MASPGPGHPW CVQSEPVQGM GVLTLLREVM LRKSPNPAHL AIAECEARLQ RQGRRVTVIT
     QNINELHYCA RSTNVLEIHG SLFKTSCMSC GNVAVSHKSP ICAALEGKGA PEPNTSDAQI
     TPHHLPRCEQ GGCSGPLRPD VVWFGETLDS DILTRVEEEL DRCDLCLVVP LPRPLWDHPA
     PCTGTP
//