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Protein

1,4-dihydroxy-2-naphthoyl-CoA synthase

Gene

menB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).UniRule annotation2 Publications

Catalytic activityi

4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H2O.UniRule annotation1 Publication

Cofactori

hydrogencarbonateUniRule annotation1 PublicationNote: The hydrogencarbonate anion plays the same catalytic role (proton acceptor) as the side-chain carboxylate group of the essential 'Asp-185' found in actinobacteria, archaea, bacteroidetes, and deltaproteobacteria.1 Publication

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

This protein is involved in step 6 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. Putative 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. no protein annotated in this organism
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei83SubstrateUniRule annotation1
Sitei83Important for catalysisUniRule annotation1
Binding sitei141SubstrateUniRule annotation1
Binding sitei147SubstrateUniRule annotation1
Binding sitei244Substrate; shared with neighboring subunitUniRule annotation1
Sitei244Important for catalysisUniRule annotation1
Binding sitei259Substrate; shared with neighboring subunitUniRule annotation1

GO - Molecular functioni

  • 1,4-dihydroxy-2-naphthoyl-CoA synthase activity Source: UniProtKB
  • bicarbonate binding Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Menaquinone biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU30800-MONOMER.
MetaCyc:MONOMER-13812.
UniPathwayiUPA00079.
UPA01057; UER00167.

Names & Taxonomyi

Protein namesi
Recommended name:
1,4-dihydroxy-2-naphthoyl-CoA synthaseUniRule annotation (EC:4.1.3.36UniRule annotation)
Short name:
DHNA-CoA synthaseUniRule annotation
Gene namesi
Name:menBUniRule annotation
Ordered Locus Names:BSU30800
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001093241 – 2711,4-dihydroxy-2-naphthoyl-CoA synthaseAdd BLAST271

Proteomic databases

PaxDbiP23966.
PRIDEiP23966.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100016756.

Structurei

3D structure databases

ProteinModelPortaliP23966.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni71 – 75Substrate bindingUniRule annotation5
Regioni115 – 119Substrate bindingUniRule annotation5
Regioni140 – 142Hydrogencarbonate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the enoyl-CoA hydratase/isomerase family. MenB subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108IPT. Bacteria.
COG0447. LUCA.
HOGENOMiHOG000027942.
InParanoidiP23966.
KOiK01661.
OMAiKYAFCSG.
PhylomeDBiP23966.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
HAMAPiMF_01934. MenB. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR010198. DHNA-CoA_synthase_MenB.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR01929. menB. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23966-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEWKTKRTY DEILYETYNG IAKITINRPE VHNAFTPKTV AEMIDAFADA
60 70 80 90 100
RDDQNVGVIV LAGAGDKAFC SGGDQKVRGH GGYVGDDQIP RLNVLDLQRL
110 120 130 140 150
IRVIPKPVVA MVSGYAIGGG HVLHIVCDLT IAADNAIFGQ TGPKVGSFDA
160 170 180 190 200
GYGSGYLARI VGHKKAREIW YLCRQYNAQE ALDMGLVNTV VPLEQLEEET
210 220 230 240 250
IKWCEEMLEK SPTALRFLKA AFNADTDGLA GIQQFAGDAT LLYYTTDEAK
260 270
EGRDSFKEKR KPDFGQFPRF P
Length:271
Mass (Da):29,899
Last modified:March 27, 2002 - v2
Checksum:iD7D74C84E35A87B0
GO

Sequence cautioni

The sequence AAA50401 differs from that shown. Reason: Frameshift at position 15.Curated
The sequence AAC37016 differs from that shown. Reason: Frameshift at position 15.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13I → D in AAA50401 (PubMed:1629163).Curated1
Sequence conflicti13I → D in AAC37016 (PubMed:8566759).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74521 Genomic DNA. Translation: AAA50401.1. Frameshift.
M74538 Genomic DNA. Translation: AAC37016.1. Frameshift.
AF008220 Genomic DNA. Translation: AAC00226.1.
AL009126 Genomic DNA. Translation: CAB15058.1.
PIRiF69656.
RefSeqiNP_390958.1. NC_000964.3.
WP_003229054.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB15058; CAB15058; BSU30800.
GeneIDi937195.
KEGGibsu:BSU30800.
PATRICi18978064. VBIBacSub10457_3220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74521 Genomic DNA. Translation: AAA50401.1. Frameshift.
M74538 Genomic DNA. Translation: AAC37016.1. Frameshift.
AF008220 Genomic DNA. Translation: AAC00226.1.
AL009126 Genomic DNA. Translation: CAB15058.1.
PIRiF69656.
RefSeqiNP_390958.1. NC_000964.3.
WP_003229054.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliP23966.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100016756.

Proteomic databases

PaxDbiP23966.
PRIDEiP23966.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15058; CAB15058; BSU30800.
GeneIDi937195.
KEGGibsu:BSU30800.
PATRICi18978064. VBIBacSub10457_3220.

Phylogenomic databases

eggNOGiENOG4108IPT. Bacteria.
COG0447. LUCA.
HOGENOMiHOG000027942.
InParanoidiP23966.
KOiK01661.
OMAiKYAFCSG.
PhylomeDBiP23966.

Enzyme and pathway databases

UniPathwayiUPA00079.
UPA01057; UER00167.
BioCyciBSUB:BSU30800-MONOMER.
MetaCyc:MONOMER-13812.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
HAMAPiMF_01934. MenB. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR010198. DHNA-CoA_synthase_MenB.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR01929. menB. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMENB_BACSU
AccessioniPrimary (citable) accession number: P23966
Secondary accession number(s): O34567
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 27, 2002
Last modified: November 30, 2016
This is version 128 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

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.