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1YFM

RECOMBINANT YEAST FUMARASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004333molecular_functionfumarate hydratase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006099biological_processtricarboxylic acid cycle
A0006106biological_processfumarate metabolic process
A0006108biological_processmalate metabolic process
A0006281biological_processDNA repair
A0006302biological_processdouble-strand break repair
A0006974biological_processDNA damage response
A0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAVE
Number of Residues1
DetailsAUTHOR STATED THIS AS MULTI-SUBUNIT ACTIVE SITE OF FUMARASE, WITH H213, T126, S124, AND N166 ALL PROVIDING HYDROGEN BONDS TO THE PUTATIVE CATALYTIC WATER MOLECULE.
ChainResidue
AHIS213

Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN
ChainResidueDetails
AGLY342-ASN351

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P05042
ChainResidueDetails
AHIS213

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P9WN93
ChainResidueDetails
ASER343

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P05042
ChainResidueDetails
ASER124
ASER164

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: in site B => ECO:0000250|UniProtKB:P05042
ChainResidueDetails
AHIS154

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WN93
ChainResidueDetails
ATHR212
ASER344
ALYS349

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000250|UniProtKB:P05042
ChainResidueDetails
AGLU356

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17761666
ChainResidueDetails
ATHR428

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
AGLU356
ASER343
ALYS349

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
ATHR212
AHIS213

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
AGLU356
ALYS349

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PDB entries from 2024-11-06

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