ASBF_BACAN
ID ASBF_BACAN Reviewed; 280 AA.
AC Q81RQ4; Q6HZY1; Q6KTW0;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=3-dehydroshikimate dehydratase {ECO:0000303|PubMed:18955706};
DE Short=3-DHS dehydratase {ECO:0000303|PubMed:18955706};
DE Short=DHSase {ECO:0000305};
DE EC=4.2.1.118 {ECO:0000269|PubMed:18955706};
DE AltName: Full=Petrobactin biosynthesis protein AsbF {ECO:0000305};
GN Name=asbF {ECO:0000303|PubMed:17189355};
GN OrderedLocusNames=BA_1986, GBAA_1986, BAS1843;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Sterne;
RX PubMed=17189355; DOI=10.1128/jb.01526-06;
RA Lee J.Y., Janes B.K., Passalacqua K.D., Pfleger B.F., Bergman N.H., Liu H.,
RA Haakansson K., Somu R.V., Aldrich C.C., Cendrowski S., Hanna P.C.,
RA Sherman D.H.;
RT "Biosynthetic analysis of the petrobactin siderophore pathway from Bacillus
RT anthracis.";
RL J. Bacteriol. 189:1698-1710(2007).
RN [5]
RP REVIEW.
RX PubMed=27425635; DOI=10.1111/mmi.13465;
RA Hagan A.K., Carlson P.E. Jr., Hanna P.C.;
RT "Flying under the radar: The non-canonical biochemistry and molecular
RT biology of petrobactin from Bacillus anthracis.";
RL Mol. Microbiol. 102:196-206(2016).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-70; ARG-102; HIS-144;
RP HIS-175; LYS-200 AND TYR-217, REACTION MECHANISM, AND ACTIVE SITE.
RC STRAIN=Sterne;
RX PubMed=18955706; DOI=10.1073/pnas.0808118105;
RA Pfleger B.F., Kim Y., Nusca T.D., Maltseva N., Lee J.Y., Rath C.M.,
RA Scaglione J.B., Janes B.K., Anderson E.C., Bergman N.H., Hanna P.C.,
RA Joachimiak A., Sherman D.H.;
RT "Structural and functional analysis of AsbF: origin of the stealth 3,4-
RT dihydroxybenzoic acid subunit for petrobactin biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:17133-17138(2008).
CC -!- FUNCTION: Involved in the biosynthesis of petrobactin, a catecholate
CC siderophore that functions in both iron acquisition and virulence
CC (PubMed:17189355, PubMed:18955706). Catalyzes the conversion of 3-
CC dehydroshikimate to 3,4-dihydroxybenzoate (3,4-DHBA) (PubMed:18955706).
CC {ECO:0000269|PubMed:17189355, ECO:0000269|PubMed:18955706}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroshikimate = 3,4-dihydroxybenzoate + H2O;
CC Xref=Rhea:RHEA:24848, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:36241; EC=4.2.1.118;
CC Evidence={ECO:0000269|PubMed:18955706};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18955706};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:18955706};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=290 uM for 3-dehydro-shikimate {ECO:0000269|PubMed:18955706};
CC pH dependence:
CC Optimum pH is >9.5. {ECO:0000269|PubMed:18955706};
CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate
CC biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 2/2.
CC -!- PATHWAY: Siderophore biosynthesis; petrobactin biosynthesis.
CC {ECO:0000269|PubMed:17189355}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18955706}.
CC -!- DISRUPTION PHENOTYPE: The deletion mutant cannot produce petrobactin on
CC iron-depleted medium. In vitro analysis show that mutants grow to a
CC very limited extent as vegetative cells in iron-depleted medium but are
CC not able to outgrow from spores under the same culture conditions.
CC {ECO:0000269|PubMed:17189355}.
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DR EMBL; AE016879; AAP25878.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT31105.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT54158.1; -; Genomic_DNA.
DR RefSeq; NP_844392.1; NC_003997.3.
DR RefSeq; WP_000877695.1; NZ_WXXJ01000029.1.
DR RefSeq; YP_028107.1; NC_005945.1.
DR PDB; 3DX5; X-ray; 2.12 A; A=1-280.
DR PDBsum; 3DX5; -.
DR AlphaFoldDB; Q81RQ4; -.
DR SMR; Q81RQ4; -.
DR STRING; 260799.BAS1843; -.
DR DNASU; 1085888; -.
DR EnsemblBacteria; AAP25878; AAP25878; BA_1986.
DR EnsemblBacteria; AAT31105; AAT31105; GBAA_1986.
DR GeneID; 45021908; -.
DR KEGG; ban:BA_1986; -.
DR KEGG; bar:GBAA_1986; -.
DR KEGG; bat:BAS1843; -.
DR PATRIC; fig|198094.11.peg.1957; -.
DR eggNOG; COG1082; Bacteria.
DR HOGENOM; CLU_086649_0_0_9; -.
DR OMA; CTITFRH; -.
DR BioCyc; MetaCyc:MON-14940; -.
DR BRENDA; 4.2.1.118; 634.
DR SABIO-RK; Q81RQ4; -.
DR UniPathway; UPA00088; UER00179.
DR UniPathway; UPA01005; -.
DR EvolutionaryTrace; Q81RQ4; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0046565; F:3-dehydroshikimate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..280
FT /note="3-dehydroshikimate dehydratase"
FT /id="PRO_0000400088"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:18955706"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18955706"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18955706"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:18955706"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18955706"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:18955706"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18955706"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18955706"
FT BINDING 198
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:18955706"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18955706"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:18955706"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18955706"
FT MUTAGEN 70
FT /note="Y->A: Binds substrate with 10-fold lower affinity;
FT when associated with A-217."
FT /evidence="ECO:0000269|PubMed:18955706"
FT MUTAGEN 102
FT /note="R->A: No activity."
FT /evidence="ECO:0000269|PubMed:18955706"
FT MUTAGEN 144
FT /note="H->A: No activity."
FT /evidence="ECO:0000269|PubMed:18955706"
FT MUTAGEN 175
FT /note="H->A: Only trace activity remaining."
FT /evidence="ECO:0000269|PubMed:18955706"
FT MUTAGEN 200
FT /note="K->A,E: No activity."
FT /evidence="ECO:0000269|PubMed:18955706"
FT MUTAGEN 200
FT /note="K->R: Less than 5% activity remaining."
FT /evidence="ECO:0000269|PubMed:18955706"
FT MUTAGEN 217
FT /note="Y->A: Binds substrate with 10-fold lower affinity;
FT when associated with A-70."
FT /evidence="ECO:0000269|PubMed:18955706"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:3DX5"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3DX5"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 79..96
FT /evidence="ECO:0007829|PDB:3DX5"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 115..134
FT /evidence="ECO:0007829|PDB:3DX5"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:3DX5"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:3DX5"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:3DX5"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:3DX5"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:3DX5"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:3DX5"
FT HELIX 259..272
FT /evidence="ECO:0007829|PDB:3DX5"
SQ SEQUENCE 280 AA; 32589 MW; EA349FA7BFDA4D98 CRC64;
MKYSLCTISF RHQLISFTDI VQFAYENGFE GIELWGTHAQ NLYMQEYETT ERELNCLKDK
TLEITMISDY LDISLSADFE KTIEKCEQLA ILANWFKTNK IRTFAGQKGS ADFSQQERQE
YVNRIRMICE LFAQHNMYVL LETHPNTLTD TLPSTLELLG EVDHPNLKIN LDFLHIWESG
ADPVDSFQQL RPWIQHYHFK NISSADYLHV FEPNNVYAAA GNRTGMVPLF EGIVNYDEII
QEVRDTDHFA SLEWFGHNAK DILKAEMKVL TNRNLEVVTS
