ASBA_BACAN
ID ASBA_BACAN Reviewed; 602 AA.
AC A0A0F7RJ52; E9QVX2; E9QVX3; Q6HZY6; Q6KTW5; Q81RQ9;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Spermidine-citrate ligase {ECO:0000305};
DE EC=6.3.2.- {ECO:0000269|PubMed:17579415, ECO:0000269|PubMed:19259597, ECO:0000269|PubMed:22408253};
DE AltName: Full=Petrobactin biosynthesis protein AsbA {ECO:0000305};
GN Name=asbA {ECO:0000303|PubMed:14756782};
GN OrderedLocusNames=GBAA_1981 {ECO:0000312|EMBL:AAT31100.1};
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 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 [2]
RP FUNCTION IN VIRULENCE, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=Sterne;
RX PubMed=14756782; DOI=10.1046/j.1365-2958.2003.03861.x;
RA Cendrowski S., MacArthur W., Hanna P.;
RT "Bacillus anthracis requires siderophore biosynthesis for growth in
RT macrophages and mouse virulence.";
RL Mol. Microbiol. 51:407-417(2004).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Sterne;
RX PubMed=16875672; DOI=10.1016/j.bbrc.2006.07.055;
RA Wilson M.K., Abergel R.J., Raymond K.N., Arceneaux J.E., Byers B.R.;
RT "Siderophores of Bacillus anthracis, Bacillus cereus, and Bacillus
RT thuringiensis.";
RL Biochem. Biophys. Res. Commun. 348:320-325(2006).
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 FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Ames;
RX PubMed=17579415; DOI=10.1021/ja072391o;
RA Oves-Costales D., Kadi N., Fogg M.J., Song L., Wilson K.S., Challis G.L.;
RT "Enzymatic logic of anthrax stealth siderophore biosynthesis: AsbA
RT catalyzes ATP-dependent condensation of citric acid and spermidine.";
RL J. Am. Chem. Soc. 129:8416-8417(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RX PubMed=19259597; DOI=10.1039/b823147h;
RA Oves-Costales D., Song L., Challis G.L.;
RT "Enantioselective desymmetrisation of citric acid catalysed by the
RT substrate-tolerant petrobactin biosynthetic enzyme AsbA.";
RL Chem. Commun. (Camb.) 11:1389-1391(2009).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=Sterne;
RX PubMed=22408253; DOI=10.1074/jbc.m112.359349;
RA Nusca T.D., Kim Y., Maltseva N., Lee J.Y., Eschenfeldt W., Stols L.,
RA Schofield M.M., Scaglione J.B., Dixon S.D., Oves-Costales D., Challis G.L.,
RA Hanna P.C., Pfleger B.F., Joachimiak A., Sherman D.H.;
RT "Functional and structural analysis of the siderophore synthetase AsbB
RT through reconstitution of the petrobactin biosynthetic pathway from
RT Bacillus anthracis.";
RL J. Biol. Chem. 287:16058-16072(2012).
RN [8]
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).
CC -!- FUNCTION: Involved in the biosynthesis of petrobactin, a catecholate
CC siderophore that functions in both iron acquisition and virulence
CC (PubMed:16875672, PubMed:17189355, PubMed:22408253). Catalyzes the ATP-
CC dependent condensation of citric acid and spermidine to form N(8)-
CC citryl-spermidine (PubMed:17579415, PubMed:19259597, PubMed:22408253).
CC It can also catalyze the condensation of several di- and triamine
CC analogs of spermidine with citric acid and the condensation of the
CC citric acid analog tricarballylic acid with spermidine
CC (PubMed:19259597). Required for growth in iron-depleted medium and for
CC full virulence in a mouse model of infection (PubMed:14756782).
CC {ECO:0000269|PubMed:14756782, ECO:0000269|PubMed:16875672,
CC ECO:0000269|PubMed:17189355, ECO:0000269|PubMed:17579415,
CC ECO:0000269|PubMed:19259597, ECO:0000269|PubMed:22408253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + citrate + spermidine = AMP + diphosphate + H(+) + N(8)-
CC citryl-spermidine; Xref=Rhea:RHEA:63808, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16947, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:149586, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:17579415, ECO:0000269|PubMed:19259597,
CC ECO:0000269|PubMed:22408253};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.65 mM for citric acid {ECO:0000269|PubMed:22408253};
CC Note=kcat is 0.89 sec(-1). {ECO:0000269|PubMed:22408253};
CC -!- PATHWAY: Siderophore biosynthesis; petrobactin biosynthesis.
CC {ECO:0000269|PubMed:17189355, ECO:0000269|PubMed:22408253}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene leads to a decrease in
CC siderophore production during iron-depleted growth and attenuates
CC growth (PubMed:14756782). The deletion mutant cannot produce
CC petrobactin on iron-depleted medium (PubMed:16875672, PubMed:17189355).
CC Mutant produces the petrobactin precursor 3,4-dihydroxybenzoyl (3,4-
CC DHB) and bacillibactin (PubMed:16875672). The deletion mutant is
CC severely attenuated for growth in macrophages and virulence in mice
CC (PubMed:14756782). In vitro analysis show that mutants grow to a very
CC limited extent as vegetative cells in iron-depleted medium but are not
CC able to outgrow from spores under the same culture conditions
CC (PubMed:17189355). {ECO:0000269|PubMed:14756782,
CC ECO:0000269|PubMed:16875672, ECO:0000269|PubMed:17189355}.
CC -!- BIOTECHNOLOGY: The ability of the enzyme to catalyze condensation of
CC citric acid with several di- and triamine analogs of spermidine
CC suggests that it may be a versatile biocatalyst for the preparation of
CC highly enantiomerically-enriched citrate derivatives via a novel type
CC of desymmetrisation process. {ECO:0000269|PubMed:19259597}.
CC -!- SIMILARITY: Belongs to the IucA/IucC family. {ECO:0000305}.
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DR EMBL; AE017334; AAT31100.1; -; Genomic_DNA.
DR RefSeq; WP_000679659.1; NZ_WXXJ01000029.1.
DR AlphaFoldDB; A0A0F7RJ52; -.
DR SMR; A0A0F7RJ52; -.
DR STRING; 260799.BAS1838; -.
DR DNASU; 1085941; -.
DR EnsemblBacteria; AAT31100; AAT31100; GBAA_1981.
DR GeneID; 45021903; -.
DR KEGG; bar:GBAA_1981; -.
DR PATRIC; fig|1392.230.peg.1941; -.
DR HOGENOM; CLU_018283_0_0_9; -.
DR OMA; TGWHRFG; -.
DR UniPathway; UPA01005; -.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR InterPro; IPR007310; Aerobactin_biosyn_IucA/IucC_N.
DR InterPro; IPR022770; FhuF_domain.
DR InterPro; IPR037455; LucA/IucC-like.
DR PANTHER; PTHR34384; PTHR34384; 1.
DR Pfam; PF06276; FhuF; 1.
DR Pfam; PF04183; IucA_IucC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..602
FT /note="Spermidine-citrate ligase"
FT /id="PRO_0000450623"
FT BINDING 286..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81RQ8"
FT BINDING 300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81RQ8"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81RQ8"
SQ SEQUENCE 602 AA; 69937 MW; C0E7182A16AE9A78 CRC64;
MKHAKQIAEH ATIQSFLNCY LRETGSGEWI TEDKRIEDIF YHLFQRDTCS TYLCCRLSAQ
NITLYGEVIY KSPTDRHLFG EQFYYQMGDS NSVMKADYVT VITFLIKEMS INYGEGTNPA
ELMLRVIRSC QNIEEFTKER KEDTSALYGF HTSFIEAEQS LLFGHLTHPT PKSRQGILEW
KSAMYSPELK GECQLHYFRA HKSIVNEKSL LLDSTTVILK EELRNDEMVS KEFISKYCNE
DEYSLLPIHP LQAEWLLHQP YVQDWIEQGV LEYIGPTGKC YMATSSLRTL YHPDAKYMLK
FSFPVKVTNS MRINKLKELE SGLEGKAMLN TAIGEVLEKF PGFDFICDPA FITLNYGTQE
SGFEVIIREN PFYSEHADDA TLIAGLVQDA IPGERTRLSN IIHRLADLES RSCEEVSLEW
FRRYMNISLK PMVWMYLQYG VALEAHQQNS VVQLKDGYPV KYYFRDNQGF YFCNSMKEML
NNELAGIGER TGNLYDDYIV DERFRYYLIF NHMFGLINGF GTAGLIREEI LLTELRTVLE
SFLPYNREPS TFLRELLEED KLACKANLLT RFFDVDELSN PLEQAIYVQV QNPLVREVAV
RS
