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2I62

Mouse Nicotinamide N-methyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006769biological_processnicotinamide metabolic process
A0008112molecular_functionnicotinamide N-methyltransferase activity
A0008168molecular_functionmethyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0016740molecular_functiontransferase activity
A0019677biological_processNAD+ catabolic process
A0032259biological_processmethylation
A0045722biological_processpositive regulation of gluconeogenesis
A0090312biological_processpositive regulation of protein deacetylation
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006769biological_processnicotinamide metabolic process
B0008112molecular_functionnicotinamide N-methyltransferase activity
B0008168molecular_functionmethyltransferase activity
B0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
B0016740molecular_functiontransferase activity
B0019677biological_processNAD+ catabolic process
B0032259biological_processmethylation
B0045722biological_processpositive regulation of gluconeogenesis
B0090312biological_processpositive regulation of protein deacetylation
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006769biological_processnicotinamide metabolic process
C0008112molecular_functionnicotinamide N-methyltransferase activity
C0008168molecular_functionmethyltransferase activity
C0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
C0016740molecular_functiontransferase activity
C0019677biological_processNAD+ catabolic process
C0032259biological_processmethylation
C0045722biological_processpositive regulation of gluconeogenesis
C0090312biological_processpositive regulation of protein deacetylation
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006769biological_processnicotinamide metabolic process
D0008112molecular_functionnicotinamide N-methyltransferase activity
D0008168molecular_functionmethyltransferase activity
D0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
D0016740molecular_functiontransferase activity
D0019677biological_processNAD+ catabolic process
D0032259biological_processmethylation
D0045722biological_processpositive regulation of gluconeogenesis
D0090312biological_processpositive regulation of protein deacetylation
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SAH A 4001
ChainResidue
ATYR12
ATYR87
ATHR88
AASN91
ACYS142
AASP143
AVAL144
ATHR164
ALEU165
AALA170
AHOH4014
ATYR21
AHOH4070
AHOH4075
ATYR26
AGLY64
ASER65
AGLY66
ATHR68
ATYR70
AASP86

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE SAH B 4002
ChainResidue
BTYR12
BTYR21
BTYR26
BGLY64
BSER65
BGLY66
BTHR68
BTYR70
BASP86
BTYR87
BTHR88
BASN91
BASP143
BVAL144
BTHR164
BLEU165
BALA170
BHOH4038

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE SAH C 4003
ChainResidue
CTYR12
CTYR21
CTYR26
CGLY64
CSER65
CGLY66
CTHR68
CTYR70
CASP86
CTYR87
CTHR88
CASN91
CCYS142
CASP143
CVAL144
CTHR145
CTHR164
CLEU165
CHOH4022
CHOH4043

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE SAH D 4004
ChainResidue
DTYR12
DTYR21
DTYR26
DGLY64
DSER65
DGLY66
DTHR68
DTYR70
DASP86
DTYR87
DTHR88
DASN91
DCYS142
DASP143
DVAL144
DTHR164
DLEU165
DHOH4026
DHOH4036

Functional Information from PROSITE/UniProt
site_idPS01100
Number of Residues17
DetailsNNMT_PNMT_TEMT NNMT/PNMT/TEMT family of methyltransferases signature. LIDIGSGPTIYQLLSAC
ChainResidueDetails
ALEU60-CYS76

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29483571","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2006","submissionDatabase":"PDB data bank","title":"The Crystal Structure of Mouse Nicotinamide N-methyltransferase in complex with SAH.","authors":["Wu H.","Min J.","Zeng H.","Loppnau P.","Weigelt J.","Sundstrom M.","Arrowsmith C.H.","Edwards A.M.","Bochkarev A.","Plotnikov A.N."]}}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P40261","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsModified residue: {"description":"Citrulline; alternate","evidences":[{"source":"UniProtKB","id":"P40261","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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