ID   ZMAJ_BACCE              Reviewed;         525 AA.
AC   Q7BQ71;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Zwittermicin A synthase ZmaJ {ECO:0000305};
DE            EC=6.2.1.72 {ECO:0000269|PubMed:16983083};
DE   AltName: Full=L-serine--[L-seryl-carrier protein] ligase {ECO:0000305};
GN   Name=zmaJ {ECO:0000303|PubMed:19098220};
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UW85;
RX   PubMed=19098220; DOI=10.1128/aem.02518-08;
RA   Kevany B.M., Rasko D.A., Thomas M.G.;
RT   "Characterization of the complete zwittermicin A biosynthesis gene cluster
RT   from Bacillus cereus.";
RL   Appl. Environ. Microbiol. 75:1144-1155(2009).
RN   [2]
RP   FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=UW85;
RX   PubMed=14711631; DOI=10.1128/aem.70.1.104-113.2004;
RA   Emmert E.A., Klimowicz A.K., Thomas M.G., Handelsman J.;
RT   "Genetics of zwittermicin a production by Bacillus cereus.";
RL   Appl. Environ. Microbiol. 70:104-113(2004).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=UW85;
RX   PubMed=16983083; DOI=10.1073/pnas.0603748103;
RA   Chan Y.A., Boyne M.T. II, Podevels A.M., Klimowicz A.K., Handelsman J.,
RA   Kelleher N.L., Thomas M.G.;
RT   "Hydroxymalonyl-acyl carrier protein (ACP) and aminomalonyl-ACP are two
RT   additional type I polyketide synthase extender units.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14349-14354(2006).
CC   -!- FUNCTION: Involved in the biosynthesis of the linear aminopolyol
CC       antibiotic zwittermicin A (ZmA) (PubMed:14711631). Specifically
CC       adenylates L-serine and loads it onto the holo form of ZmaH via a
CC       thioester linkage to the phosphopanthetheine moiety (PubMed:16983083).
CC       {ECO:0000269|PubMed:14711631, ECO:0000269|PubMed:16983083}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + holo-[peptidyl-carrier protein] + L-serine = AMP +
CC         diphosphate + L-seryl-[peptidyl-carrier protein];
CC         Xref=Rhea:RHEA:61704, Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:15913,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:144955, ChEBI:CHEBI:456215;
CC         EC=6.2.1.72; Evidence={ECO:0000269|PubMed:16983083};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61705;
CC         Evidence={ECO:0000269|PubMed:16983083};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.8 mM for L-serine {ECO:0000269|PubMed:16983083};
CC         Note=kcat is 42 min(-1). {ECO:0000269|PubMed:16983083};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:14711631}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene abolishes ZmA production.
CC       {ECO:0000269|PubMed:14711631}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; FJ430564; AAR87759.1; -; Genomic_DNA.
DR   RefSeq; WP_065229817.1; NZ_LYVD01000026.1.
DR   BioCyc; MetaCyc:MON-19434; -.
DR   BRENDA; 6.2.1.72; 648.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020459; AMP-binding.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PRINTS; PR00154; AMPBINDING.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..525
FT                   /note="Zwittermicin A synthase ZmaJ"
FT                   /id="PRO_0000454893"
SQ   SEQUENCE   525 AA;  58770 MW;  8EC54FAA77E8BA11 CRC64;
     MSTCIQKLFE EQVVRTPDEV AVIFKKETLT YKELNEKSNQ LARLLREGGV GPDTVVGIMV
     ERSIEMVVGI FGILKAGGAY LPLSPNHPSS RLQFIIEDSG AKLILTQKQI LHRFQDSLKA
     DMLALDSISY EGKGENLECI NKPSDLVYVI YTSGSTGKPK GVMIEHSALI NRIEWMQEAY
     PISSKDTILQ KTPYTFDVSV WEMFWWAIVG AKVCILAPGM EKFPQAIIET TESNDVTIMH
     FVPSMLSAFL HYLDVTGETN RIKSLKQVFV SGEALLSQHI NRFNKLLNFS NGTLLTNLYG
     PTEATIDVTA YDCPTHEITE GSVPIGRPIK NIEMFVVDKY GNKLPEGHIG ELCISGIGLA
     RGYVNRPQLT AEKFVQYSLD TRIYKTGDLA LIRSDGNIEF HGRIDFQVKV NGLRIELGEI
     ESCLMSCEGV LQCAVIVRQE SEMVVKLIAF YESENDIELE RLKKYLRLFL PDYMIPNSFV
     RVNEMPLTDS GKIDRKVLAL LGSDKYSHHT TLVGGSVNEE SSKDS