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Protein

2-succinylbenzoate--CoA ligase

Gene

menE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA).UniRule annotation1 Publication

Catalytic activityi

ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 2-succinylbenzoyl-CoA.UniRule annotation

Pathwayi: 1,4-dihydroxy-2-naphthoate biosynthesis

This protein is involved in step 5 of the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate.UniRule annotation
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Isochorismate synthase MenF (menF)
  2. 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (menD)
  3. 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (menH)
  4. o-succinylbenzoate synthase (menC)
  5. 2-succinylbenzoate--CoA ligase (menE)
  6. 1,4-dihydroxy-2-naphthoyl-CoA synthase (menB)
  7. 1,4-dihydroxy-2-naphthoyl-CoA hydrolase (menI)
This subpathway is part of the pathway 1,4-dihydroxy-2-naphthoate biosynthesis, which is itself part of Quinol/quinone metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate, the pathway 1,4-dihydroxy-2-naphthoate biosynthesis and in Quinol/quinone metabolism.

Pathwayi: menaquinone biosynthesis

This protein is involved in the pathway menaquinone biosynthesis, which is part of Quinol/quinone metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway menaquinone biosynthesis and in Quinol/quinone metabolism.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • o-succinylbenzoate-CoA ligase activity Source: EcoliWiki

GO - Biological processi

  • menaquinone biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Menaquinone biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:O-SUCCINYLBENZOATE-COA-LIG-MONOMER.
ECOL316407:JW2255-MONOMER.
MetaCyc:O-SUCCINYLBENZOATE-COA-LIG-MONOMER.
UniPathwayiUPA00079.
UPA01057; UER00166.

Names & Taxonomyi

Protein namesi
Recommended name:
2-succinylbenzoate--CoA ligaseUniRule annotation (EC:6.2.1.26UniRule annotation)
Alternative name(s):
o-succinylbenzoyl-CoA synthetaseUniRule annotation
Short name:
OSB-CoA synthetaseUniRule annotation
Gene namesi
Name:menEUniRule annotation
Ordered Locus Names:b2260, JW2255
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12437. menE.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001931751 – 4512-succinylbenzoate--CoA ligaseAdd BLAST451

Proteomic databases

PaxDbiP37353.
PRIDEiP37353.

Interactioni

Protein-protein interaction databases

BioGridi4262001. 15 interactors.
DIPiDIP-10186N.
IntActiP37353. 4 interactors.
STRINGi511145.b2260.

Structurei

Secondary structure

1451
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Helixi7 – 15Combined sources9
Beta strandi18 – 23Combined sources6
Beta strandi26 – 29Combined sources4
Helixi30 – 46Combined sources17
Beta strandi54 – 58Combined sources5
Helixi63 – 74Combined sources12
Beta strandi78 – 82Combined sources5
Helixi88 – 94Combined sources7
Helixi95 – 97Combined sources3
Beta strandi102 – 104Combined sources3
Beta strandi115 – 118Combined sources4
Beta strandi135 – 141Combined sources7
Beta strandi151 – 155Combined sources5
Helixi156 – 167Combined sources12
Beta strandi177 – 179Combined sources3
Helixi187 – 199Combined sources13
Beta strandi202 – 205Combined sources4
Helixi211 – 214Combined sources4
Turni215 – 217Combined sources3
Beta strandi219 – 223Combined sources5
Helixi225 – 234Combined sources10
Beta strandi241 – 245Combined sources5
Helixi252 – 260Combined sources9
Beta strandi265 – 271Combined sources7
Helixi272 – 274Combined sources3
Beta strandi276 – 282Combined sources7
Beta strandi296 – 301Combined sources6
Beta strandi304 – 309Combined sources6
Beta strandi314 – 318Combined sources5
Beta strandi321 – 323Combined sources3
Beta strandi332 – 341Combined sources10
Beta strandi344 – 350Combined sources7
Helixi351 – 353Combined sources3
Beta strandi355 – 357Combined sources3
Beta strandi360 – 362Combined sources3
Helixi364 – 371Combined sources8
Beta strandi377 – 387Combined sources11
Beta strandi391 – 403Combined sources13
Helixi410 – 413Combined sources4
Helixi417 – 419Combined sources3
Beta strandi422 – 426Combined sources5
Helixi440 – 448Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5C5HX-ray2.40A/B1-451[»]
ProteinModelPortaliP37353.
SMRiP37353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family. MenE subfamily.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000230003.
InParanoidiP37353.
KOiK01911.
OMAiFRASARC.
PhylomeDBiP37353.

Family and domain databases

CDDicd05912. OSB_CoA_lg. 1 hit.
HAMAPiMF_00731. MenE. 1 hit.
InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR010192. MenE.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01923. menE. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37353-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIFSDWPWRH WRQVRGETIA LRLNDEQLNW RELCARVDEL ASGFAVQGVV
60 70 80 90 100
EGSGVMLRAW NTPQTLLAWL ALLQCGARVL PVNPQLPQPL LEELLPNLTL
110 120 130 140 150
QFALVPDGEN TFPALTSLHI QLVEGAHAAT WQPTRLCSMT LTSGSTGLPK
160 170 180 190 200
AAVHTYQAHL ASAQGVLSLI PFGDHDDWLL SLPLFHVSGQ GIMWRWLYAG
210 220 230 240 250
ARMTVRDKQP LEQMLAGCTH ASLVPTQLWR LLVNRSSVSL KAVLLGGAAI
260 270 280 290 300
PVELTEQARE QGIRCFCGYG LTEFASTVCA KEADGLADVG SPLPGREVKI
310 320 330 340 350
VNNEVWLRAA SMAEGYWRNG QLVSLVNDEG WYATRDRGEM HNGKLTIVGR
360 370 380 390 400
LDNLFFSGGE GIQPEEVERV IAAHPAVLQV FIVPVADKEF GHRPVAVMEY
410 420 430 440 450
DHESVDLSEW VKDKLARFQQ PVRWLTLPPE LKNGGIKISR QALKEWVQRQ

Q
Length:451
Mass (Da):50,185
Last modified:November 1, 1997 - v2
Checksum:i2009B8092984EFB2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti382I → N in AAB04893 (PubMed:8626063).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35031 Genomic DNA. Translation: AAB04893.1.
U00096 Genomic DNA. Translation: AAC75320.1.
AP009048 Genomic DNA. Translation: BAA16084.1.
PIRiB64997.
RefSeqiNP_416763.1. NC_000913.3.
WP_000577625.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75320; AAC75320; b2260.
BAA16084; BAA16084; BAA16084.
GeneIDi946741.
KEGGiecj:JW2255.
eco:b2260.
PATRICi32119887. VBIEscCol129921_2353.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35031 Genomic DNA. Translation: AAB04893.1.
U00096 Genomic DNA. Translation: AAC75320.1.
AP009048 Genomic DNA. Translation: BAA16084.1.
PIRiB64997.
RefSeqiNP_416763.1. NC_000913.3.
WP_000577625.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5C5HX-ray2.40A/B1-451[»]
ProteinModelPortaliP37353.
SMRiP37353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262001. 15 interactors.
DIPiDIP-10186N.
IntActiP37353. 4 interactors.
STRINGi511145.b2260.

Proteomic databases

PaxDbiP37353.
PRIDEiP37353.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75320; AAC75320; b2260.
BAA16084; BAA16084; BAA16084.
GeneIDi946741.
KEGGiecj:JW2255.
eco:b2260.
PATRICi32119887. VBIEscCol129921_2353.

Organism-specific databases

EchoBASEiEB2332.
EcoGeneiEG12437. menE.

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000230003.
InParanoidiP37353.
KOiK01911.
OMAiFRASARC.
PhylomeDBiP37353.

Enzyme and pathway databases

UniPathwayiUPA00079.
UPA01057; UER00166.
BioCyciEcoCyc:O-SUCCINYLBENZOATE-COA-LIG-MONOMER.
ECOL316407:JW2255-MONOMER.
MetaCyc:O-SUCCINYLBENZOATE-COA-LIG-MONOMER.

Miscellaneous databases

PROiP37353.

Family and domain databases

CDDicd05912. OSB_CoA_lg. 1 hit.
HAMAPiMF_00731. MenE. 1 hit.
InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR010192. MenE.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01923. menE. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMENE_ECOLI
AccessioniPrimary (citable) accession number: P37353
Secondary accession number(s): P78178, P78253
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.