ARMT1_DANRE
ID ARMT1_DANRE Reviewed; 448 AA.
AC Q58EM4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
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};
GN ORFNames=zgc:110816 {ECO:0000303|Ref.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2005) 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; BC091842; AAH91842.1; -; mRNA.
DR RefSeq; NP_001014353.1; NM_001014331.2.
DR AlphaFoldDB; Q58EM4; -.
DR SMR; Q58EM4; -.
DR STRING; 7955.ENSDARP00000072525; -.
DR PaxDb; Q58EM4; -.
DR DNASU; 541518; -.
DR Ensembl; ENSDART00000078062; ENSDARP00000072525; ENSDARG00000055676.
DR GeneID; 541518; -.
DR KEGG; dre:541518; -.
DR CTD; 79624; -.
DR ZFIN; ZDB-GENE-050327-51; armt1.
DR eggNOG; KOG3870; Eukaryota.
DR GeneTree; ENSGT00530000064023; -.
DR HOGENOM; CLU_030117_2_1_1; -.
DR InParanoid; Q58EM4; -.
DR OMA; GFRPTNI; -.
DR OrthoDB; 856818at2759; -.
DR PhylomeDB; Q58EM4; -.
DR TreeFam; TF314853; -.
DR PRO; PR:Q58EM4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000055676; Expressed in tail and 22 other tissues.
DR ExpressionAtlas; Q58EM4; baseline.
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:0016791; F:phosphatase activity; IBA:GO_Central.
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..448
FT /note="Damage-control phosphatase ARMT1"
FT /id="PRO_0000230798"
FT MOTIF 405..408
FT /note="Subfamily III RTxK motif"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 257..258
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 257
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
FT BINDING 295
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 295
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
FT BINDING 371..375
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 408
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
SQ SEQUENCE 448 AA; 51776 MW; D9682E4DF894A89E CRC64;
MEAEGMLPPQ SLSAKFEGSF AYLTVRDRLP TILTKVVDTL HRNKDNFYKE YGEEGTEAEK
RAISFLSRLR NELQTDKPVL ALTDNAEDTQ AWNEYMERQQ DLMENGQLVS WFKSPWLYVE
CYMYRRIQEA LYMNPPMHNF DPFKEGKTQS YFESQQAIKY LCTYLQELIT NMENMTEIQL
RENFLKLIQV SLWGNKCDLS ISAGQDNSQK LSPIDSLPDL QRFILVDDSS MVWSTLVASQ
GSRSSGMKHA RVDIILDNAG FELVTDLVLA DFLISSGLAK QIRFHGKSIP WFVSDVTKQD
FEWTIKQTMA ANHKWMSASG VQWKHFMKEG TWSYHDHPFW TLPHEFCDMT VDAANLYSTL
QTSDLILFKG DLNYRKLTGD RKWEHTVRFD QALRGFQPAP LCSLRTLKAD VQVGLQAGHA
EKLSTQDPDW MTNGKYAVVQ FSSPHREQ
