ID A0A1S3SJ74_SALSA Unreviewed; 784 AA.
AC A0A1S3SJ74;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase-like isoform X1 {ECO:0000313|RefSeq:XP_014064392.1};
GN Name=LOC106609886 {ECO:0000313|RefSeq:XP_014064392.1};
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_014064392.1};
RN [1] {ECO:0000313|RefSeq:XP_014064392.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014064392.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014064392.1; XM_014208917.1.
DR AlphaFoldDB; A0A1S3SJ74; -.
DR STRING; 8030.ENSSSAP00000005436; -.
DR PaxDb; 8030-ENSSSAP00000005436; -.
DR Ensembl; ENSSSAT00000135355; ENSSSAP00000100849; ENSSSAG00000002513.
DR GeneID; 106609886; -.
DR KEGG; sasa:106609886; -.
DR OMA; RIMKCIN; -.
DR OrthoDB; 5489121at2759; -.
DR Proteomes; UP000087266; Chromosome ssa08.
DR Bgee; ENSSSAG00000002513; Expressed in heart and 14 other cell types or tissues.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:InterPro.
DR CDD; cd03786; GTB_UDP-GlcNAc_2-Epimerase; 1.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR InterPro; IPR020004; UDP-GlcNAc_Epase.
DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR NCBIfam; TIGR03568; NeuC_NnaA; 1.
DR PANTHER; PTHR18964:SF149; BIFUNCTIONAL UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE_N-ACETYLMANNOSAMINE KINASE; 1.
DR PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1.
DR Pfam; PF02350; Epimerase_2; 1.
DR Pfam; PF00480; ROK; 1.
DR PRINTS; PR00475; HEXOKINASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|RefSeq:XP_014064392.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000313|RefSeq:XP_014064392.1}.
FT DOMAIN 96..434
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 578
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-1"
FT BINDING 630
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 640
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 642
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
SQ SEQUENCE 784 AA; 86791 MW; 7FD20E4641035C06 CRC64;
MIRREGKRPK KGGERGSSER ERERSGSRSG LTMRPRPIGR NPHELYYLRM QRMREKTDKM
EESKAMRKLR VCVATCNRAD YSKLAPIMFG IKANPDEFEL EVVVLGSHLI DDYGNTFRMI
EQDDFDIGSK LHTIVRGEDE AAMVESVGLA LVKLPDVLHR LRPDVLVVHG DRFDALALAT
AAALMNIRIL HLEGGEVSGT IDDSIRHAIS KLAHYHACCT RTAEQHLIAM CEDHTRILLA
GCPSYDKLLA AHHRDDYMDI IRNWLGDNVK EDNYIVALQH PVTTDIKNSI KIYELMLDAL
ISFNKRTLVL FPNIDAGSKE MVRVMRKKGV EQHPNFRAVK HVPFEQFIQL VCHAGAMIGN
SSCGVREAGA FGTPVINLGS RQTGRETGEN VLHVRDADTQ NKIYHALELQ FGKRYPCSKI
YGDGNAVPRI LKFLQTIDLD EPLQKTFCFP PVKEWDISQD IDHILETQSA LAVDLGGTNL
RVAIVSMRGK IVKKYTQTNP KTYEARIELI LKMCTEAVFD AVHLNCRILG VGVSTGGRVN
PQEGVILHST KLIQEWSSID IRTPISDALH LPIWVDNDGN CAALAEKKFG HGKGVENFVT
IITGTGIGGG IIQHNELIHG STFCAAELGH IMVSLDGPEC MCGSRGCIEA YASGMALQKE
AKRLHDEELL EVEGMVDLKK AESISAIHLI NAARLGNRKA EAVLRTAGMA LGVGIVNILH
MVNPSLVILS GVLAAHYQAP VQQVIDQRAL TSAQGIQVLT SDLEEPALLG AASMVLDYTT
RRIY
//
