Q81RQ4 (ASBF_BACAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-dehydroshikimate dehydratase
Short name=3-DHS dehydratase
Short name=DHSase
EC=4.2.1.118

Alternative name(s):
Petrobactin biosynthesis protein AsbF

Gene names

Name:	asbF
Ordered Locus Names:	BA_1986, GBAA_1986, BAS1843

Organism

Bacillus anthracis [Reference proteome] [HAMAP]

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	280 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts 3-dehydroshikimate to protocatechuate (3,4-dihydroxybenzoate), a biosynthetic unit required for the biosynthesis of petrobactin which is a virulence-associated siderophore produced by B.anthracis. Ref.4
Catalytic activity	3-dehydro-shikimate = protocatechuate + H2O. Ref.4
Cofactor	Binds 1 manganese ion per subunit. Ref.4
Pathway	Aromatic compound metabolism; 3,4-dihydroxybenzoate biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 2/2. Siderophore biosynthesis; petrobactin biosynthesis.
Subunit structure	Homodimer. Ref.4
Biophysicochemical properties	Kinetic parameters: KM=290 µM for 3-dehydro-shikimate Ref.4 pH dependence: Optimum pH is >9.5.

Ontologies

Keywords
Ligand	Manganese Metal-binding
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	lyase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding 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 – 280

280

3-dehydroshikimate dehydratase

PRO_0000400088

Sites

Active site

144

1

Proton acceptor

Metal binding

142

1

Manganese

Metal binding

172

1

Manganese

Metal binding

198

1

Manganese

Metal binding

253

1

Manganese

Binding site

70

1

Substrate

Binding site

102

1

Substrate

Binding site

142

1

Substrate

Binding site

172

1

Substrate

Binding site

175

1

Substrate

Binding site

217

1

Substrate

Binding site

253

1

Substrate

Experimental info

Mutagenesis

70

1

Y → A: Binds substrate with 10-fold lower affinity; when associagted with A-217. Ref.4

Mutagenesis

102

1

R → A: No activity. Ref.4

Mutagenesis

144

1

H → A: No activity. Ref.4

Mutagenesis

175

1

H → A: Only trace activity remaining. Ref.4

Mutagenesis

200

1

K → A or E: No activity. Ref.4

Mutagenesis

200

1

K → R: Less than 5% activity remaining. Ref.4

Mutagenesis

217

1

Y → A: Binds substrate with 10-fold lower affinity; when associagted with A-70. Ref.4

Secondary structure

1

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280

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

7 – 10

4

Helix

17 – 26

10

Beta strand

31 – 35

5

Helix

36 – 45

10

Helix

47 – 56

10

Helix

58 – 60

3

Beta strand

64 – 68

5

Helix

79 – 96

18

Beta strand

100 – 103

4

Helix

110 – 112

3

Helix

115 – 134

20

Beta strand

138 – 142

5

Helix

152 – 162

11

Beta strand

167 – 172

6

Helix

173 – 178

6

Helix

183 – 190

8

Helix

191 – 193

3

Beta strand

194 – 199

6

Beta strand

201 – 203

3

Helix

205 – 211

7

Helix

213 – 217

5

Helix

229 – 231

3

Beta strand

232 – 234

3

Helix

236 – 243

8

Beta strand

249 – 252

4

Helix

259 – 272

14

Sequences

	Sequence		Length	Mass (Da)
	Q81RQ4 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: EA349FA7BFDA4D98	FASTA	280	32,589
	10 20 30 40 50 60 MKYSLCTISF RHQLISFTDI VQFAYENGFE GIELWGTHAQ NLYMQEYETT ERELNCLKDK 70 80 90 100 110 120 TLEITMISDY LDISLSADFE KTIEKCEQLA ILANWFKTNK IRTFAGQKGS ADFSQQERQE 130 140 150 160 170 180 YVNRIRMICE LFAQHNMYVL LETHPNTLTD TLPSTLELLG EVDHPNLKIN LDFLHIWESG 190 200 210 220 230 240 ADPVDSFQQL RPWIQHYHFK NISSADYLHV FEPNNVYAAA GNRTGMVPLF EGIVNYDEII 250 260 270 280 QEVRDTDHFA SLEWFGHNAK DILKAEMKVL TNRNLEVVTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'." Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A. J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.
[4]	"Structural and functional analysis of AsbF: origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis." Pfleger B.F., Kim Y., Nusca T.D., Maltseva N., Lee J.Y., Rath C.M., Scaglione J.B., Janes B.K., Anderson E.C., Bergman N.H., Hanna P.C., Joachimiak A., Sherman D.H. Proc. Natl. Acad. Sci. U.S.A. 105:17133-17138(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-70; ARG-102; HIS-144; HIS-175; LYS-200 AND TYR-217, REACTION MECHANISM. Strain: Sterne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE016879 Genomic DNA. Translation: AAP25878.1.
AE017334 Genomic DNA. Translation: AAT31105.1.
AE017225 Genomic DNA. Translation: AAT54158.1.

RefSeq

NP_844392.1. NC_003997.3.
YP_018630.1. NC_007530.2.
YP_028107.1. NC_005945.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DX5	X-ray	2.12	A	1-280	[»]

ProteinModelPortal

Q81RQ4.

ModBase

Search...

Protein-protein interaction databases

STRING

198094.BA_1986.

Protocols and materials databases

DNASU

1085888.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAP25878; AAP25878; BA_1986.
AAT31105; AAT31105; GBAA_1986.
AAT54158; AAT54158; BAS1843.

GeneID

1085888.
2815037.
2848581.

KEGG

ban:BA_1986.
bar:GBAA_1986.
bat:BAS1843.

Phylogenomic databases

eggNOG

NOG11361.

HOGENOM

HOG000088353.

KO

K15652.

OMA

VWEGGDD.

ProtClustDB

CLSK916442.

Enzyme and pathway databases

BioCyc

BANT260799:GJAJ-1912-MONOMER.
BANT261594:GJ7F-1987-MONOMER.
MetaCyc:MONOMER-14940.

UniPathway

UPA00088; UER00179.
UPA01005.

Family and domain databases

Gene3D

3.20.20.150. 1 hit.

InterPro

IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]

Pfam

PF01261. AP_endonuc_2. 1 hit.
[Graphical view]

SUPFAM

SSF51658. Xyl_isomerase-like_TIM-brl. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q81RQ4.

Entry information

Entry name

ASBF_BACAN

Accession

Primary (citable) accession number: Q81RQ4
Secondary accession number(s): Q6HZY1, Q6KTW0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2010
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program