GAL1_TREPA
ID GAL1_TREPA Reviewed; 397 AA.
AC O83433;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Putative galactokinase;
DE EC=2.7.1.6;
DE AltName: Full=Galactose kinase;
GN Name=galK; OrderedLocusNames=TP_0418;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
CC -!- FUNCTION: Catalyzes the transfer of the gamma-phosphate of ATP to D-
CC galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate
CC + H(+); Xref=Rhea:RHEA:13553, ChEBI:CHEBI:15378, ChEBI:CHEBI:28061,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58336, ChEBI:CHEBI:456216; EC=2.7.1.6;
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000520; AAC65405.1; -; Genomic_DNA.
DR PIR; H71327; H71327.
DR AlphaFoldDB; O83433; -.
DR SMR; O83433; -.
DR IntAct; O83433; 9.
DR STRING; 243276.TPANIC_0418; -.
DR EnsemblBacteria; AAC65405; AAC65405; TP_0418.
DR KEGG; tpa:TP_0418; -.
DR eggNOG; COG0153; Bacteria.
DR HOGENOM; CLU_017814_2_1_12; -.
DR OMA; PVCYNLR; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004335; F:galactokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR InterPro; IPR000705; Galactokinase.
DR InterPro; IPR019539; GalKase_N.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006206; Mevalonate/galactokinase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10457:SF6; PTHR10457:SF6; 1.
DR Pfam; PF10509; GalKase_gal_bdg; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR PIRSF; PIRSF000530; Galactokinase; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
PE 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; Cytoplasm; Galactose metabolism;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..397
FT /note="Putative galactokinase"
FT /id="PRO_0000184634"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 38
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 397 AA; 45255 MW; A86D102B89C6FB6C CRC64;
MLYYFNTLAM MLRMQRVESC HTEEYGDEPE AIAVVPGRFH LLGEYLWFAQ GNTLSMAIDQ
TLTLCVSRRK DSTFRLFSLT LGERRKISTA NLRYRKEDRW ANSVKAVILS FMDGGYHLTG
LNCTILSQIP PDAGLGTPNA LKVAMALVLG RLFAATLPKE SVVSIVEHAN ERYLKTHAHR
ADILCVLFAK QGSCVRTDHR KKQAELCQFP SEGKRIVLTD SRVPRFIARE EFTARLKRCV
DAYELVKRNP DMPRAMSKLM AAALEEIDVP EGIRRRVISL VRESLGVDEA IEALRKRDFA
AFSRVVNRSH ERLRDRFEIS CPELDWLVKR ALEFVDPDAP DVVCSRLTGR GFGGCTYAIL
RDQDFEPYLE RLDEYERIFG FKAAAYEVQC SEGARVL