P1254_THEMA
ID P1254_THEMA Reviewed; 216 AA.
AC Q9X0Y1;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Phosphorylated carbohydrates phosphatase TM_1254;
DE EC=3.1.3.-;
GN OrderedLocusNames=TM_1254;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, COFACTOR, AND KINETIC PARAMETERS.
RX PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT "Enzyme genomics: application of general enzymatic screens to discover new
RT enzymes.";
RL FEMS Microbiol. Rev. 29:263-279(2005).
CC -!- FUNCTION: Displays high phosphatase activity toward erythrose 4-
CC phosphate, fructose 6-phosphate, 2-deoxyglucose 6-phosphate, and
CC mannose 6-phosphate. May have a role in the intracellular metabolism of
CC many phosphorylated carbohydrates. {ECO:0000269|PubMed:15808744}.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:15808744};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15808744};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15808744};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:15808744};
CC Note=Divalent metal cation. Highest activity with Co(2+), followed by
CC Mg(2+), Mn(2+) or Ni(2+). {ECO:0000269|PubMed:15808744};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=152 uM for erythrose 4-phosphate {ECO:0000269|PubMed:15808744};
CC KM=0.2 mM for fructose 6-phosphate {ECO:0000269|PubMed:15808744};
CC Vmax=2.63 umol/min/mg enzyme with erythrose 4-phosphate as substrate
CC {ECO:0000269|PubMed:15808744};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD36329.1; -; Genomic_DNA.
DR PIR; H72277; H72277.
DR RefSeq; NP_229059.1; NC_000853.1.
DR RefSeq; WP_004080009.1; NZ_CP011107.1.
DR PDB; 3KBB; X-ray; 1.74 A; A=1-216.
DR PDBsum; 3KBB; -.
DR AlphaFoldDB; Q9X0Y1; -.
DR SMR; Q9X0Y1; -.
DR STRING; 243274.THEMA_08065; -.
DR DNASU; 898229; -.
DR EnsemblBacteria; AAD36329; AAD36329; TM_1254.
DR KEGG; tma:TM1254; -.
DR eggNOG; COG0637; Bacteria.
DR InParanoid; Q9X0Y1; -.
DR OMA; YHGRRPM; -.
DR OrthoDB; 1167152at2; -.
DR BRENDA; 3.1.3.58; 6331.
DR EvolutionaryTrace; Q9X0Y1; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cobalt; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Nickel; Reference proteome.
FT CHAIN 1..216
FT /note="Phosphorylated carbohydrates phosphatase TM_1254"
FT /id="PRO_0000058124"
FT ACT_SITE 7
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3KBB"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 64..82
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:3KBB"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3KBB"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:3KBB"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3KBB"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:3KBB"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:3KBB"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:3KBB"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3KBB"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:3KBB"
SQ SEQUENCE 216 AA; 24629 MW; 20A89F394A36E9EA CRC64;
MEAVIFDMDG VLMDTEPLYF EAYRRVAESY GKPYTEDLHR RIMGVPEREG LPILMEALEI
KDSLENFKKR VHEEKKRVFS ELLKENPGVR EALEFVKSKR IKLALATSTP QREALERLRR
LDLEKYFDVM VFGDQVKNGK PDPEIYLLVL ERLNVVPEKV VVFEDSKSGV EAAKSAGIER
IYGVVHSLND GKALLEAGAV ALVKPEEILN VLKEVL
