Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2-succinylbenzoate--CoA ligase

Gene

menE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

GO - Biological processi

  • menaquinone biosynthetic process Source: EcoCyc
  • protein homotetramerization Source: EcoCyc

Keywordsi

Molecular functionLigase
Biological processMenaquinone biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:O-SUCCINYLBENZOATE-COA-LIG-MONOMER
MetaCyc:O-SUCCINYLBENZOATE-COA-LIG-MONOMER
UniPathwayi
UPA00079

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4262001, 15 interactors
DIPiDIP-10186N
IntActiP37353, 4 interactors
STRINGi316385.ECDH10B_2421

Structurei

Secondary structure

1451
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
OMAiVHNVQAH
PhylomeDBiP37353

Family and domain databases

CDDicd05912 OSB_CoA_lg, 1 hit
HAMAPiMF_00731 MenE, 1 hit
InterProiView protein in InterPro
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR010192 MenE
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
TIGRFAMsiTIGR01923 menE, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit

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
PATRICifig|1411691.4.peg.4476

Similar proteinsi

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
STRINGi316385.ECDH10B_2421

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
PATRICifig|1411691.4.peg.4476

Organism-specific databases

EchoBASEiEB2332
EcoGeneiEG12437 menE

Phylogenomic databases

eggNOGiENOG4105CEY Bacteria
COG0318 LUCA
HOGENOMiHOG000230003
InParanoidiP37353
KOiK01911
OMAiVHNVQAH
PhylomeDBiP37353

Enzyme and pathway databases

UniPathwayi
UPA00079

UPA01057;UER00166

BioCyciEcoCyc:O-SUCCINYLBENZOATE-COA-LIG-MONOMER
MetaCyc:O-SUCCINYLBENZOATE-COA-LIG-MONOMER

Miscellaneous databases

PROiPR:P37353

Family and domain databases

CDDicd05912 OSB_CoA_lg, 1 hit
HAMAPiMF_00731 MenE, 1 hit
InterProiView protein in InterPro
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR010192 MenE
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
TIGRFAMsiTIGR01923 menE, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMENE_ECOLI
AccessioniPrimary (citable) accession number: P37353
Secondary accession number(s): P78178, P78253
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 139 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again