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6MEL

Succinyl-CoA synthase from Campylobacter jejuni

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004775molecular_functionsuccinate-CoA ligase (ADP-forming) activity
A0004776molecular_functionsuccinate-CoA ligase (GDP-forming) activity
A0006099biological_processtricarboxylic acid cycle
A0009361cellular_componentsuccinate-CoA ligase complex (ADP-forming)
A0016874molecular_functionligase activity
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004775molecular_functionsuccinate-CoA ligase (ADP-forming) activity
B0004776molecular_functionsuccinate-CoA ligase (GDP-forming) activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006099biological_processtricarboxylic acid cycle
B0006104biological_processsuccinyl-CoA metabolic process
B0016874molecular_functionligase activity
B0042709cellular_componentsuccinate-CoA ligase complex
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CL A 601
ChainResidue
ASER154
AGLY155
AHIS247
AHOH788
BALA266
BGLY267

site_idAC2
Number of Residues13
Detailsbinding site for residue CIT B 501
ChainResidue
BGLY291
BGLY292
BGLY321
BILE322
BVAL323
BHOH636
BHOH666
BHOH675
BHOH677
BHOH684
AHOH796
BASN264
BGLY290

Functional Information from PROSITE/UniProt
site_idPS00399
Number of Residues14
DetailsSUCCINYL_COA_LIG_2 ATP-citrate lyase / succinyl-CoA ligases family active site. GatApkgk...RMGHAG
ChainResidueDetails
AGLY236-GLY249

site_idPS01216
Number of Residues30
DetailsSUCCINYL_COA_LIG_1 ATP-citrate lyase / succinyl-CoA ligases family signature 1. SKSGTLTyEaanqvvqggyGistaVGIGGD
ChainResidueDetails
ASER152-ASP181

site_idPS01217
Number of Residues25
DetailsSUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GdVacMvNGAGLAmatmDiInys.GA
ChainResidueDetails
BGLY257-ALA281

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00558
ChainResidueDetails
BLYS46
BGLY53
BGLU99
BALA102
BGLU107
BASN199
BASP213
BASN264
BGLY321

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PDB entries from 2024-07-24

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