ID   GALK2_PONAB             Reviewed;         458 AA.
AC   Q5R6J8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=N-acetylgalactosamine kinase;
DE            EC=2.7.1.157;
DE   AltName: Full=GalNAc kinase;
DE   AltName: Full=Galactokinase 2;
GN   Name=GALK2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts on GalNAc. Also acts as a galactokinase when galactose
CC       is present at high concentrations (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + N-acetyl-alpha-D-galactosamine = ADP + H(+) + N-acetyl-
CC         alpha-D-galactosamine 1-phosphate; Xref=Rhea:RHEA:12617,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:40356,
CC         ChEBI:CHEBI:61970, ChEBI:CHEBI:456216; EC=2.7.1.157;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR860491; CAH92612.1; -; mRNA.
DR   RefSeq; NP_001126530.1; NM_001133058.1.
DR   AlphaFoldDB; Q5R6J8; -.
DR   SMR; Q5R6J8; -.
DR   STRING; 9601.ENSPPYP00000007322; -.
DR   Ensembl; ENSPPYT00000007624; ENSPPYP00000007322; ENSPPYG00000006463.
DR   GeneID; 100173519; -.
DR   KEGG; pon:100173519; -.
DR   CTD; 2585; -.
DR   eggNOG; KOG0631; Eukaryota.
DR   eggNOG; KOG3885; Eukaryota.
DR   GeneTree; ENSGT00950000183187; -.
DR   InParanoid; Q5R6J8; -.
DR   OrthoDB; 860024at2759; -.
DR   Proteomes; UP000001595; Chromosome 15.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004335; F:galactokinase activity; IEA:Ensembl.
DR   GO; GO:0033858; F:N-acetylgalactosamine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR000705; Galactokinase.
DR   InterPro; IPR019741; Galactokinase_CS.
DR   InterPro; IPR019539; GalKase_N.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR   InterPro; IPR006206; Mevalonate/galactokinase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   Pfam; PF10509; GalKase_gal_bdg; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF000530; Galactokinase; 1.
DR   PRINTS; PR00473; GALCTOKINASE.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
DR   TIGRFAMs; TIGR00131; gal_kin; 1.
DR   PROSITE; PS00106; GALACTOKINASE; 1.
DR   PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..458
FT                   /note="N-acetylgalactosamine kinase"
FT                   /id="PRO_0000184649"
FT   ACT_SITE        190
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         49..52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         139..149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         187..190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            43
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   458 AA;  50351 MW;  1EC42CD918278EC6 CRC64;
     MATESPATRR VQVAEHPRLL KLKEMFNSKF GSIPKFYVRA PGRVNIIGEH IDYCGYSVLP
     MAVEQDVLIA VEPVKTYTLQ LANTNPLYPD LSTSANNIQI DKTKPLWHNY FLCGLKGIQE
     HFGVSNLTGM NCLVDGNIPP SSGLSSSSAL VCCAGLVTLT VLGRNLSKVE LAEICAKSER
     YIGTEGGGMD QSISFLAEEG TAKLIEFSPL RATDVKLPSG AVFVIANSCV EMNKAATSHF
     NIRVMECRLA AKLLAKYKSL QWDKVLRLEE VQAKLGISLE EMLLVTEDAL HPEPYNPEEI
     CRCLGISLEE LRTQILSPNT QDVLIFKLYQ RAKHVYSEAA RVLQFKKICE EAPENMVQLL
     GELMNQSHMS CRDMYECSCP ELDQLVDICR KFGAQGSRLT GAGWGGCTVS IVPADKLPSF
     LANVHKAYYH RSDGSLAPEK QSLFATKPGG GALVLLEA