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

2,3-dihydroxybenzoate-AMP ligase

Gene

dhbE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the catecholic siderophore bacillibactin. Catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate.1 Publication

Pathwayi: bacillibactin biosynthesis

This protein is involved in the pathway bacillibactin biosynthesis, which is part of Siderophore biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway bacillibactin biosynthesis and in Siderophore biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei191ATP; via carbonyl oxygen1 Publication1
Binding sitei240Substrate1 Publication1
Binding sitei307ATP; via amide nitrogen1 Publication1
Binding sitei329ATP; via carbonyl oxygen1 Publication1
Binding sitei413ATP1 Publication1
Binding sitei428ATP1 Publication1
Binding sitei519ATP1 Publication1
Binding sitei519Substrate1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU31980-MONOMER.
MetaCyc:MONOMER-13920.
SABIO-RKP40871.
UniPathwayiUPA00013.

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-dihydroxybenzoate-AMP ligase1 Publication (EC:6.3.2.-)
Alternative name(s):
Dihydroxybenzoic acid-activating enzyme
Gene namesi
Name:dhbE1 Publication
Synonyms:entE
Ordered Locus Names:BSU31980
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001930741 – 5392,3-dihydroxybenzoate-AMP ligaseAdd BLAST539

Proteomic databases

PaxDbiP40871.

Interactioni

Protein-protein interaction databases

IntActiP40871. 1 interactor.
MINTiMINT-8366125.
STRINGi224308.Bsubs1_010100017366.

Structurei

Secondary structure

1539
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 18Combined sources9
Helixi27 – 38Combined sources12
Beta strandi41 – 46Combined sources6
Beta strandi49 – 52Combined sources4
Helixi53 – 70Combined sources18
Beta strandi77 – 80Combined sources4
Beta strandi84 – 86Combined sources3
Helixi87 – 98Combined sources12
Beta strandi101 – 104Combined sources4
Helixi111 – 120Combined sources10
Beta strandi124 – 132Combined sources9
Helixi137 – 147Combined sources11
Beta strandi154 – 158Combined sources5
Beta strandi163 – 165Combined sources3
Helixi166 – 168Combined sources3
Beta strandi183 – 189Combined sources7
Beta strandi193 – 196Combined sources4
Beta strandi199 – 203Combined sources5
Helixi204 – 218Combined sources15
Beta strandi225 – 228Combined sources4
Helixi235 – 239Combined sources5
Helixi242 – 248Combined sources7
Beta strandi252 – 255Combined sources4
Beta strandi257 – 260Combined sources4
Helixi261 – 271Combined sources11
Beta strandi274 – 278Combined sources5
Helixi280 – 292Combined sources13
Beta strandi302 – 308Combined sources7
Helixi312 – 315Combined sources4
Helixi318 – 321Combined sources4
Beta strandi324 – 331Combined sources8
Beta strandi337 – 339Combined sources3
Beta strandi342 – 344Combined sources3
Helixi346 – 351Combined sources6
Beta strandi355 – 358Combined sources4
Beta strandi362 – 366Combined sources5
Beta strandi379 – 384Combined sources6
Helixi396 – 402Combined sources7
Beta strandi409 – 417Combined sources9
Beta strandi419 – 421Combined sources3
Beta strandi423 – 428Combined sources6
Helixi429 – 431Combined sources3
Beta strandi433 – 435Combined sources3
Beta strandi438 – 440Combined sources3
Helixi442 – 449Combined sources8
Beta strandi455 – 465Combined sources11
Turni466 – 468Combined sources3
Beta strandi469 – 481Combined sources13
Helixi485 – 494Combined sources10
Helixi499 – 501Combined sources3
Beta strandi504 – 508Combined sources5
Helixi522 – 534Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MD9X-ray2.80A1-539[»]
1MDBX-ray2.15A1-539[»]
1MDFX-ray2.50A1-539[»]
ProteinModelPortaliP40871.
SMRiP40871.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40871.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni234 – 235Substrate binding1 Publication2

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108IQC. Bacteria.
COG1021. LUCA.
HOGENOMiHOG000230011.
InParanoidiP40871.
KOiK02363.
OMAiVGGAKCS.
PhylomeDBiP40871.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR011963. DHB_AMP_lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02275. DHB_AMP_lig. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40871-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKGFTPWPD ELAETYRKNG CWAGETFGDL LRDRAAKYGD RIAITCGNTH
60 70 80 90 100
WSYRELDTRA DRLAAGFQKL GIQQMDRVVV QLPNIKEFFE VIFALFRLGA
110 120 130 140 150
LPVFALPSHR SSEITYFCEF AEAAAYIIPD AYSGFDYRSL ARQVQSKLPT
160 170 180 190 200
LKNIIVAGEA EEFLPLEDLH AEPVKLPEVK SSDVAFLQLS GGSTGLSKLI
210 220 230 240 250
PRTHDDYIYS LKRSVEVCWL DHSTVYLAAL PMAHNYPLSS PGVLGVLYAG
260 270 280 290 300
GRVVLSPSPS PDDAFPLIER EKVTITALVP PLAMVWMDAA SSRRDDLSSL
310 320 330 340 350
QVLQVGGAKF SAEAARRVKA VFGCTLQQVF GMAEGLVNYT RLDDPEEIIV
360 370 380 390 400
NTQGKPMSPY DEMRVWDDHD RDVKPGETGH LLTRGPYTIR GYYKAEEHNA
410 420 430 440 450
ASFTEDGFYR TGDIVRLTRD GYIVVEGRAK DQINRGGEKV AAEEVENHLL
460 470 480 490 500
AHPAVHDAAM VSMPDQFLGE RSCVFIIPRD EAPKAAELKA FLRERGLAAY
510 520 530
KIPDRVEFVE SFPQTGVGKV SKKALREAIS EKLLAGFKK
Length:539
Mass (Da):59,928
Last modified:November 1, 1995 - v2
Checksum:i027D286940B192F8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti360Y → I in AAA79759 (PubMed:8224884).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26444 Genomic DNA. Translation: AAC44632.1.
AL009126 Genomic DNA. Translation: CAB15188.1.
L08645 Genomic DNA. Translation: AAA79759.1.
PIRiD69615.
RefSeqiNP_391078.1. NC_000964.3.
WP_003243083.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15188; CAB15188; BSU31980.
GeneIDi936509.
KEGGibsu:BSU31980.
PATRICi18978368. VBIBacSub10457_3347.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26444 Genomic DNA. Translation: AAC44632.1.
AL009126 Genomic DNA. Translation: CAB15188.1.
L08645 Genomic DNA. Translation: AAA79759.1.
PIRiD69615.
RefSeqiNP_391078.1. NC_000964.3.
WP_003243083.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MD9X-ray2.80A1-539[»]
1MDBX-ray2.15A1-539[»]
1MDFX-ray2.50A1-539[»]
ProteinModelPortaliP40871.
SMRiP40871.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP40871. 1 interactor.
MINTiMINT-8366125.
STRINGi224308.Bsubs1_010100017366.

Proteomic databases

PaxDbiP40871.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15188; CAB15188; BSU31980.
GeneIDi936509.
KEGGibsu:BSU31980.
PATRICi18978368. VBIBacSub10457_3347.

Phylogenomic databases

eggNOGiENOG4108IQC. Bacteria.
COG1021. LUCA.
HOGENOMiHOG000230011.
InParanoidiP40871.
KOiK02363.
OMAiVGGAKCS.
PhylomeDBiP40871.

Enzyme and pathway databases

UniPathwayiUPA00013.
BioCyciBSUB:BSU31980-MONOMER.
MetaCyc:MONOMER-13920.
SABIO-RKP40871.

Miscellaneous databases

EvolutionaryTraceiP40871.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR011963. DHB_AMP_lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02275. DHB_AMP_lig. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDHBE_BACSU
AccessioniPrimary (citable) accession number: P40871
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 121 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.