ARMT1_XENLA
ID ARMT1_XENLA Reviewed; 440 AA.
AC Q6AXB1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Damage-control phosphatase ARMT1 {ECO:0000250|UniProtKB:Q04371};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q04371};
DE AltName: Full=Acidic residue methyltransferase 1 {ECO:0000250|UniProtKB:Q9H993};
DE AltName: Full=Protein-glutamate O-methyltransferase {ECO:0000250|UniProtKB:Q9H993};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9H993};
DE AltName: Full=Sugar phosphate phosphatase ARMT1 {ECO:0000250|UniProtKB:Q04371};
GN Name=armt1 {ECO:0000250|UniProtKB:Q9H993};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Metal-dependent phosphatase that shows phosphatase activity
CC against several substrates, including fructose-1-phosphate and
CC fructose-6-phosphate (By similarity). Its preference for fructose-1-
CC phosphate, a strong glycating agent that causes DNA damage rather than
CC a canonical yeast metabolite, suggests a damage-control function in
CC hexose phosphate metabolism (By similarity). Has also been shown to
CC have O-methyltransferase activity that methylates glutamate residues of
CC target proteins to form gamma-glutamyl methyl ester residues (By
CC similarity). Possibly methylates PCNA, suggesting it is involved in the
CC DNA damage response (By similarity). {ECO:0000250|UniProtKB:Q04371,
CC ECO:0000250|UniProtKB:Q9H993}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate;
CC Xref=Rhea:RHEA:35603, ChEBI:CHEBI:15377, ChEBI:CHEBI:37721,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:138881;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate +
CC dihydroxyacetone; Xref=Rhea:RHEA:28002, ChEBI:CHEBI:16016,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:59776;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; Evidence={ECO:0000250|UniProtKB:Q9H993};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- DOMAIN: Subfamily III proteins have a conserved RTxK motif about 40-50
CC residues from the C-terminus; the threonine may be replaced by serine
CC or cysteine. {ECO:0000250|UniProtKB:Q04371}.
CC -!- PTM: Automethylated. {ECO:0000250|UniProtKB:Q9H993}.
CC -!- SIMILARITY: Belongs to the damage-control phosphatase family. Sugar
CC phosphate phosphatase III subfamily. {ECO:0000305}.
CC -!- CAUTION: Human C6orf211 has been reportedly associated with a protein
CC carboxyl methyltransferase activity, but whether this protein indeed
CC has such an activity remains to be determined (By similarity). It has
CC been later shown to belong to a family of metal-dependent phosphatases
CC implicated in metabolite damage-control (By similarity).
CC {ECO:0000250|UniProtKB:Q9H993}.
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DR EMBL; BC079682; AAH79682.1; -; mRNA.
DR RefSeq; NP_001087371.1; NM_001093902.1.
DR AlphaFoldDB; Q6AXB1; -.
DR SMR; Q6AXB1; -.
DR MaxQB; Q6AXB1; -.
DR DNASU; 447195; -.
DR GeneID; 447195; -.
DR KEGG; xla:447195; -.
DR CTD; 447195; -.
DR Xenbase; XB-GENE-6254320; armt1.L.
DR OMA; LFMEMCE; -.
DR OrthoDB; 856818at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 447195; Expressed in zone of skin and 19 other tissues.
DR GO; GO:0097023; F:fructose 6-phosphate aldolase activity; IEA:RHEA.
DR GO; GO:0103026; F:fructose-1-phosphatase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051998; F:protein carboxyl O-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:RHEA.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; ISS:UniProtKB.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; ISS:UniProtKB.
DR InterPro; IPR036075; ARMT-1-like_metal-bd_sf.
DR InterPro; IPR039763; ARMT1.
DR InterPro; IPR002791; ARMT1-like_metal-bd.
DR PANTHER; PTHR12260; PTHR12260; 1.
DR Pfam; PF01937; ARMT1-like_dom; 1.
DR SUPFAM; SSF111321; SSF111321; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Manganese; Metal-binding; Methyltransferase; Nickel;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..440
FT /note="Damage-control phosphatase ARMT1"
FT /id="PRO_0000358926"
FT MOTIF 400..403
FT /note="Subfamily III RTxK motif"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 252..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 257
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
FT BINDING 290
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 290
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
FT BINDING 366..370
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
SQ SEQUENCE 440 AA; 50680 MW; 1FE1FE3149ABEABF CRC64;
MDPPCSLSAS FEGSFAYLTV RDRLPQILTK VIDTVHRNKH KFFEDHGEEG VEAEKRALSF
FSKLRNEMQT NKPVLPLTDN QLDTELWNQY LDYQKSLLNE GETPSWFKSP WLYVECYMYR
RIQEGIVLSP PISKYDVFRE GKIESFFQSQ PAIIALCTYL QELKKNMAAL SENQKQEELY
KLLQVCLWGN KCDLSISGGL DNSQKFSILS SLESFRPFIL VNDMESVLSV LLESKNPESG
KELMKRVDIV LDNAGFELIT DFVLADALLS FRLASEVHFH GKCMPWFVSD TTKHDFNWTI
KQLQAANHKW MSKCGGNWKE NLKKSHWIYH EHPFWTLPHE FCMMAQTAPD LYSELQKSDL
VIFKGDLNYR KLTGDRKWDF TVPFSEALTT FHPAPLCSIR TLKADVQVGL KAGIGEQLFS
TEPDWMISGK YGVVQLSTSV
