P40871 (DHBE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2,3-dihydroxybenzoate-AMP ligase
EC=6.3.2.-

Alternative name(s):
Dihydroxybenzoic acid-activating enzyme

Gene names

Name:	dhbE
Synonyms:	entE
Ordered Locus Names:	BSU31980

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	539 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate.
Pathway	Siderophore biosynthesis; bacillibactin biosynthesis.
Subcellular location	Cytoplasm Potential.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	siderophore biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	(2,3-dihydroxybenzoyl)adenylate synthase activity Inferred from electronic annotation. Source: InterPro ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ligase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 539

539

2,3-dihydroxybenzoate-AMP ligase

PRO_0000193074

Regions

Nucleotide binding

191 – 192

2

ATP

Nucleotide binding

307 – 309

3

ATP

Region

234 – 235

2

Substrate binding

Sites

Binding site

240

1

Substrate

Binding site

329

1

ATP; via carbonyl oxygen

Binding site

413

1

ATP

Binding site

428

1

ATP

Binding site

519

1

ATP

Binding site

519

1

Substrate

Experimental info

Sequence conflict

360

1

Y → I in AAA79759. Ref.3

Secondary structure

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539

Helix Strand Turn

Details...

Helix

10 – 18

9

Helix

27 – 38

12

Beta strand

41 – 46

6

Beta strand

49 – 52

4

Helix

53 – 70

18

Beta strand

77 – 80

4

Beta strand

84 – 86

3

Helix

87 – 98

12

Beta strand

101 – 104

4

Helix

111 – 120

10

Beta strand

124 – 132

9

Helix

137 – 147

11

Beta strand

154 – 158

5

Beta strand

163 – 165

3

Helix

166 – 168

3

Beta strand

183 – 189

7

Beta strand

193 – 196

4

Beta strand

199 – 203

5

Helix

204 – 218

15

Beta strand

225 – 228

4

Helix

235 – 239

5

Helix

242 – 248

7

Beta strand

252 – 255

4

Beta strand

257 – 260

4

Helix

261 – 271

11

Beta strand

274 – 278

5

Helix

280 – 292

13

Beta strand

302 – 308

7

Helix

312 – 315

4

Helix

318 – 321

4

Beta strand

324 – 331

8

Beta strand

337 – 339

3

Beta strand

342 – 344

3

Helix

346 – 351

6

Beta strand

355 – 358

4

Beta strand

362 – 366

5

Beta strand

379 – 384

6

Helix

396 – 402

7

Beta strand

409 – 417

9

Beta strand

419 – 421

3

Beta strand

423 – 428

6

Helix

429 – 431

3

Beta strand

433 – 435

3

Beta strand

438 – 440

3

Helix

442 – 449

8

Beta strand

455 – 465

11

Turn

466 – 468

3

Beta strand

469 – 481

13

Helix

485 – 494

10

Helix

499 – 501

3

Beta strand

504 – 508

5

Helix

522 – 534

13

Sequences

	Sequence		Length	Mass (Da)
	P40871 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 027D286940B192F8	FASTA	539	59,928
	10 20 30 40 50 60 MLKGFTPWPD ELAETYRKNG CWAGETFGDL LRDRAAKYGD RIAITCGNTH WSYRELDTRA 70 80 90 100 110 120 DRLAAGFQKL GIQQMDRVVV QLPNIKEFFE VIFALFRLGA LPVFALPSHR SSEITYFCEF 130 140 150 160 170 180 AEAAAYIIPD AYSGFDYRSL ARQVQSKLPT LKNIIVAGEA EEFLPLEDLH AEPVKLPEVK 190 200 210 220 230 240 SSDVAFLQLS GGSTGLSKLI PRTHDDYIYS LKRSVEVCWL DHSTVYLAAL PMAHNYPLSS 250 260 270 280 290 300 PGVLGVLYAG GRVVLSPSPS PDDAFPLIER EKVTITALVP PLAMVWMDAA SSRRDDLSSL 310 320 330 340 350 360 QVLQVGGAKF SAEAARRVKA VFGCTLQQVF GMAEGLVNYT RLDDPEEIIV NTQGKPMSPY 370 380 390 400 410 420 DEMRVWDDHD RDVKPGETGH LLTRGPYTIR GYYKAEEHNA ASFTEDGFYR TGDIVRLTRD 430 440 450 460 470 480 GYIVVEGRAK DQINRGGEKV AAEEVENHLL AHPAVHDAAM VSMPDQFLGE RSCVFIIPRD 490 500 510 520 530 EAPKAAELKA FLRERGLAAY KIPDRVEFVE SFPQTGVGKV SKKALREAIS EKLLAGFKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and genetic organization of a Bacillus subtilis operon encoding 2,3-dihydroxybenzoate biosynthetic enzymes." Rowland B.M., Grossman T.H., Osburne M.S., Taber H.W. Gene 178:119-123(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Cloning and mapping of the Bacillus subtilis locus homologous to Escherichia coli ent genes." Adams R., Schumann W. Gene 133:119-121(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 341-533. Strain: 168.
[4]	"Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases." May J.J., Kessler N., Marahiel M.A., Stubbs M.T. Proc. Natl. Acad. Sci. U.S.A. 99:12120-12125(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEXES WITH AMP AND 2,3-DIHYDROXYBENZOATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U26444 Genomic DNA. Translation: AAC44632.1.
AL009126 Genomic DNA. Translation: CAB15188.1.
L08645 Genomic DNA. Translation: AAA79759.1.

PIR

D69615.

RefSeq

NP_391078.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MD9	X-ray	2.80	A	1-539	[»]
1MDB	X-ray	2.15	A	1-539	[»]
1MDF	X-ray	2.50	A	1-539	[»]

ProteinModelPortal

P40871.

SMR

P40871. Positions 1-536.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU31980.

Proteomic databases

PaxDb

P40871.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB15188; CAB15188; BSU31980.

GeneID

936509.

KEGG

bsu:BSU31980.

PATRIC

18978368. VBIBacSub10457_3347.

Organism-specific databases

GenoList

BSU31980. [Micado]

Phylogenomic databases

eggNOG

COG1021.

HOGENOM

HOG000230011.

KO

K02363.

OMA

KMFLRER.

ProtClustDB

CLSK887818.

Enzyme and pathway databases

BioCyc

BSUB:BSU31980-MONOMER.
MetaCyc:MONOMER-13920.

UniPathway

UPA00013.

Family and domain databases

InterPro

IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR011963. DHB_AMP_lig.
IPR025110. DUF4009.
[Graphical view]

Pfam

PF00501. AMP-binding. 1 hit.
PF13193. DUF4009. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02275. DHB_AMP_lig. 1 hit.

PROSITE

PS00455. AMP_BINDING. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00131. Adenosine monophosphate.

EvolutionaryTrace

P40871.

Entry information

Entry name

DHBE_BACSU

Accession

Primary (citable) accession number: P40871

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program