eF-site ID 1fuq-AB
PDB Code 1fuq
Chain A, B

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Title FUMARASE WITH BOUND 3-TRIMETHYLSILYLSUCCINIC ACID
Classification LYASE
Compound FUMARASE C
Source Escherichia coli (strain K12) (FUMC_ECOLI)
Sequence A:  VRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTS
LIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLAG
QHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRG
MERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQLIPQ
LKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISG
WVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYA
RRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKG
LAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPG
KVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRP
MVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLN
ESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALG
YLSEAEFDSWVRPEQM
B:  MNTVRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKM
PTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEV
LAGQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGG
VRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQL
IPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQE
ISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHP
EYARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGA
LKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPMPGK
VNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPM
VIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNE
SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGY
LSEAEFDSWVRPEQM
Description


Functional site
1) chain A
residue 126
type
sequence R
description BINDING SITE FOR RESIDUE SIF A 1000
source : AC1
2) chain A
residue 129
type
sequence H
description BINDING SITE FOR RESIDUE SIF A 1000
source : AC1
3) chain A
residue 130
type
sequence P
description BINDING SITE FOR RESIDUE SIF A 1000
source : AC1
4) chain A
residue 131
type
sequence N
description BINDING SITE FOR RESIDUE SIF A 1000
source : AC1
5) chain A
residue 132
type
sequence D
description BINDING SITE FOR RESIDUE SIF A 1000
source : AC1
6) chain A
residue 100
type
sequence T
description BINDING SITE FOR RESIDUE CIT A 1001
source : AC2
7) chain A
residue 139
type
sequence S
description BINDING SITE FOR RESIDUE CIT A 1001
source : AC2
8) chain A
residue 140
type
sequence S
description BINDING SITE FOR RESIDUE CIT A 1001
source : AC2
9) chain A
residue 141
type
sequence N
description BINDING SITE FOR RESIDUE CIT A 1001
source : AC2
10) chain A
residue 324
type
sequence K
description BINDING SITE FOR RESIDUE CIT A 1001
source : AC2
11) chain A
residue 326
type
sequence N
description BINDING SITE FOR RESIDUE CIT A 1001
source : AC2
12) chain B
residue 187
type
sequence T
description BINDING SITE FOR RESIDUE CIT A 1001
source : AC2
13) chain B
residue 188
type
sequence H
description BINDING SITE FOR RESIDUE CIT A 1001
source : AC2
14) chain B
residue 126
type
sequence R
description BINDING SITE FOR RESIDUE SIF B 1001
source : AC3
15) chain B
residue 129
type
sequence H
description BINDING SITE FOR RESIDUE SIF B 1001
source : AC3
16) chain B
residue 130
type
sequence P
description BINDING SITE FOR RESIDUE SIF B 1001
source : AC3
17) chain B
residue 131
type
sequence N
description BINDING SITE FOR RESIDUE SIF B 1001
source : AC3
18) chain B
residue 132
type
sequence D
description BINDING SITE FOR RESIDUE SIF B 1001
source : AC3
19) chain A
residue 187
type
sequence T
description BINDING SITE FOR RESIDUE CIT B 1002
source : AC4
20) chain A
residue 188
type
sequence H
description BINDING SITE FOR RESIDUE CIT B 1002
source : AC4
21) chain B
residue 100
type
sequence T
description BINDING SITE FOR RESIDUE CIT B 1002
source : AC4
22) chain B
residue 139
type
sequence S
description BINDING SITE FOR RESIDUE CIT B 1002
source : AC4
23) chain B
residue 140
type
sequence S
description BINDING SITE FOR RESIDUE CIT B 1002
source : AC4
24) chain B
residue 141
type
sequence N
description BINDING SITE FOR RESIDUE CIT B 1002
source : AC4
25) chain B
residue 324
type
sequence K
description BINDING SITE FOR RESIDUE CIT B 1002
source : AC4
26) chain B
residue 326
type
sequence N
description BINDING SITE FOR RESIDUE CIT B 1002
source : AC4
27) chain A
residue 188
type catalytic
sequence H
description 569
source MCSA : MCSA1
28) chain A
residue 318
type catalytic
sequence S
description 569
source MCSA : MCSA1
29) chain A
residue 324
type catalytic
sequence K
description 569
source MCSA : MCSA1
30) chain A
residue 331
type catalytic
sequence E
description 569
source MCSA : MCSA1
31) chain B
residue 188
type catalytic
sequence H
description 569
source MCSA : MCSA2
32) chain B
residue 324
type catalytic
sequence K
description 569
source MCSA : MCSA2
33) chain B
residue 331
type catalytic
sequence E
description 569
source MCSA : MCSA2
34) chain A
residue 98
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:12021453, ECO:0000305|PubMed:8909293, ECO:0000305|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1KQ7, ECO:0007744|PDB:2FUS
source Swiss-Prot : SWS_FT_FI3
35) chain B
residue 98
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:12021453, ECO:0000305|PubMed:8909293, ECO:0000305|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1KQ7, ECO:0007744|PDB:2FUS
source Swiss-Prot : SWS_FT_FI3
36) chain A
residue 126
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1FUR
source Swiss-Prot : SWS_FT_FI4
37) chain B
residue 126
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1FUR
source Swiss-Prot : SWS_FT_FI4
38) chain A
residue 188
type ACT_SITE
sequence H
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:9098893
source Swiss-Prot : SWS_FT_FI1
39) chain B
residue 188
type ACT_SITE
sequence H
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:9098893
source Swiss-Prot : SWS_FT_FI1
40) chain A
residue 318
type ACT_SITE
sequence S
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00743
source Swiss-Prot : SWS_FT_FI2
41) chain A
residue 129
type BINDING
sequence H
description in site B => ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1FUR, ECO:0007744|PDB:1KQ7
source Swiss-Prot : SWS_FT_FI5
42) chain B
residue 129
type BINDING
sequence H
description in site B => ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1FUR, ECO:0007744|PDB:1KQ7
source Swiss-Prot : SWS_FT_FI5
43) chain A
residue 317-326
type prosite
sequence GSSIMPGKVN
description FUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN
source prosite : PS00163
44) chain A
residue 139
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1KQ7, ECO:0007744|PDB:2FUS
source Swiss-Prot : SWS_FT_FI6
45) chain B
residue 139
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1KQ7, ECO:0007744|PDB:2FUS
source Swiss-Prot : SWS_FT_FI6
46) chain A
residue 187
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00743
source Swiss-Prot : SWS_FT_FI7
47) chain A
residue 319
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00743
source Swiss-Prot : SWS_FT_FI7
48) chain A
residue 324
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00743
source Swiss-Prot : SWS_FT_FI7
49) chain B
residue 187
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00743
source Swiss-Prot : SWS_FT_FI7
50) chain B
residue 324
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00743
source Swiss-Prot : SWS_FT_FI7
51) chain A
residue 331
type SITE
sequence E
description Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:8909293
source Swiss-Prot : SWS_FT_FI8
52) chain B
residue 331
type SITE
sequence E
description Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:8909293
source Swiss-Prot : SWS_FT_FI8

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