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5D6B

Human fumarase (wild type)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000050biological_processurea cycle
A0003824molecular_functioncatalytic activity
A0004333molecular_functionfumarate hydratase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006099biological_processtricarboxylic acid cycle
A0006106biological_processfumarate metabolic process
A0006108biological_processmalate metabolic process
A0006281biological_processDNA repair
A0006525biological_processarginine metabolic process
A0006974biological_processDNA damage response
A0016829molecular_functionlyase activity
A0070062cellular_componentextracellular exosome
A0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN
ChainResidueDetails
AGLY364-ASN373

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P9WN93","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"description":"in site B","evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P9WN93","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues7
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P97807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P97807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P97807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PRKDC","evidences":[{"source":"PubMed","id":"26237645","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P97807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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