(data stored in SCRATCH3701 zone)

SWISSPROT: D5E9D0_METMS

ID   D5E9D0_METMS            Unreviewed;       227 AA.
AC   D5E9D0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 51.
DE   RecName: Full=Phosphoglycolate phosphatase {ECO:0000256|HAMAP-Rule:MF_01419};
DE            Short=PGP {ECO:0000256|HAMAP-Rule:MF_01419};
DE            Short=PGPase {ECO:0000256|HAMAP-Rule:MF_01419};
DE            EC=3.1.3.18 {ECO:0000256|HAMAP-Rule:MF_01419};
GN   OrderedLocusNames=Mmah_0249 {ECO:0000313|EMBL:ADE35781.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35781.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35781.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dephosphorylation of 2-phosphoglycolate.
CC       {ECO:0000256|HAMAP-Rule:MF_01419}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-phosphoglycolate + H2O = glycolate + phosphate;
CC         Xref=Rhea:RHEA:14369, ChEBI:CHEBI:15377, ChEBI:CHEBI:29805,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58033; EC=3.1.3.18;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01419};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01419};
CC   -!- SIMILARITY: Belongs to the archaeal SPP-like hydrolase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01419}.
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DR   EMBL; CP001994; ADE35781.1; -; Genomic_DNA.
DR   EnsemblBacteria; ADE35781; ADE35781; Mmah_0249.
DR   KEGG; mmh:Mmah_0249; -.
DR   eggNOG; arCOG01213; Archaea.
DR   eggNOG; COG0561; LUCA.
DR   HOGENOM; HOG000184780; -.
DR   KO; K22223; -.
DR   OMA; DTGYAYH; -.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_01419; GPH_hydrolase_arch; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006382; PGPase.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E9D0.
DR   SWISS-2DPAGE; D5E9D0.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01419};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01419, ECO:0000313|EMBL:ADE35781.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01419};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01419};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   ACT_SITE        10
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT   METAL           10
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT   METAL           12
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT   METAL           174
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT   METAL           178
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT   BINDING         151
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
SQ   SEQUENCE   227 AA;  24773 MW;  34E70C66821FB91A CRC64;
     MMKFKALAID IDGTITYSDR RLHFLAAEHL RNLGIPVVLA TGNVLCYAAA TSKLIGLGGK
     VISENGGVIS TGFDTNPHIS ESMEECEKAF SYLSNRFDLI RLDGDLRKTE IALRRNVNAD
     DLQASLEGAG FYIEVIDTQF ALHIKSKKVN KGTGLEKMAS LMDLDVSDFI AIGDSVNDRE
     MFEVAGYGIA VDNADPGLKL IADHVTSMSF GEGTVEALQI LCRRDFF
//

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