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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12437. menE.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4514512-succinylbenzoate--CoA ligasePRO_0000193175Add
BLAST

Proteomic databases

PaxDbiP37353.
PRIDEiP37353.

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

1
451
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Helixi7 – 159Combined sources
Beta strandi18 – 236Combined sources
Beta strandi26 – 294Combined sources
Helixi30 – 4617Combined sources
Beta strandi54 – 585Combined sources
Helixi63 – 7412Combined sources
Beta strandi78 – 825Combined sources
Helixi88 – 947Combined sources
Helixi95 – 973Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi115 – 1184Combined sources
Beta strandi135 – 1417Combined sources
Beta strandi151 – 1555Combined sources
Helixi156 – 16712Combined sources
Beta strandi177 – 1793Combined sources
Helixi187 – 19913Combined sources
Beta strandi202 – 2054Combined sources
Helixi211 – 2144Combined sources
Turni215 – 2173Combined sources
Beta strandi219 – 2235Combined sources
Helixi225 – 23410Combined sources
Beta strandi241 – 2455Combined sources
Helixi252 – 2609Combined sources
Beta strandi265 – 2717Combined sources
Helixi272 – 2743Combined sources
Beta strandi276 – 2827Combined sources
Beta strandi296 – 3016Combined sources
Beta strandi304 – 3096Combined sources
Beta strandi314 – 3185Combined sources
Beta strandi321 – 3233Combined sources
Beta strandi332 – 34110Combined sources
Beta strandi344 – 3507Combined sources
Helixi351 – 3533Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi360 – 3623Combined sources
Helixi364 – 3718Combined sources
Beta strandi377 – 38711Combined sources
Beta strandi391 – 40313Combined sources
Helixi410 – 4134Combined sources
Helixi417 – 4193Combined sources
Beta strandi422 – 4265Combined sources
Helixi440 – 4489Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5C5HX-ray2.40A/B1-451[»]
ProteinModelPortaliP37353.
SMRiP37353. Positions 1-451.
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

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti382 – 3821I → N in AAB04893 (PubMed:8626063).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
5C5HX-ray2.40A/B1-451[»]
ProteinModelPortaliP37353.
SMRiP37353. Positions 1-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262001. 15 interactions.
DIPiDIP-10186N.
IntActiP37353. 4 interactions.
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

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: September 7, 2016
This is version 132 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.