ID   ACVS_STRCL              Reviewed;         805 AA.
AC   Q01757;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase;
DE            EC=6.3.2.26;
DE   AltName: Full=Delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase;
DE            Short=ACV synthetase;
DE            Short=ACVS;
DE   Flags: Fragment;
GN   Name=pcbAB;
OS   Streptomyces clavuligerus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7881554; DOI=10.1099/13500872-140-12-3367;
RA   Yu H., Serpe E., Romero J., Coque J.J., Maeda K., Oelgeschlager M.,
RA   Hintermann G., Liras P., Martin J.F., Demain A.L., Piret J.;
RT   "Possible involvement of the lysine epsilon-aminotransferase gene (lat) in
RT   the expression of the genes encoding ACV synthetase (pcbAB) and
RT   isopenicillin N synthase (pcbC) in Streptomyces clavuligerus.";
RL   Microbiology 140:3367-3377(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-293.
RX   PubMed=1917855; DOI=10.1128/jb.173.19.6223-6229.1991;
RA   Tobin M.B., Kovacevic S., Madduri K., Hoskins J.A., Skatrud P.L.,
RA   Vining L.C., Stuttard C., Miller J.R.;
RT   "Localization of the lysine epsilon-aminotransferase (lat) and delta-(L-
RT   alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase (pcbAB) genes from
RT   Streptomyces clavuligerus and production of lysine epsilon-aminotransferase
RT   activity in Escherichia coli.";
RL   J. Bacteriol. 173:6223-6229(1991).
CC   -!- FUNCTION: Each of the constituent amino acids of ACV are activated as
CC       aminoacyl-adenylates with peptide bonds formed through the
CC       participation of amino acid thioester intermediates.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 ATP + H2O + L-2-aminoadipate + L-cysteine + L-valine = 3 AMP
CC         + 3 diphosphate + 3 H(+) + N-[(5S)-5-amino-5-carboxypentanoyl]-L-
CC         cysteinyl-D-valine; Xref=Rhea:RHEA:23196, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:57762, ChEBI:CHEBI:58572,
CC         ChEBI:CHEBI:58672, ChEBI:CHEBI:456215; EC=6.3.2.26;
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000305};
CC       Note=Binds 3 phosphopantetheines covalently. {ECO:0000305};
CC   -!- PATHWAY: Antibiotic biosynthesis; penicillin G biosynthesis; penicillin
CC       G from L-alpha-aminoadipate and L-cysteine and L-valine: step 1/3.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; U12015; AAB39900.1; -; Genomic_DNA.
DR   EMBL; M64834; AAA26778.1; -; Genomic_DNA.
DR   PIR; B38169; B38169.
DR   AlphaFoldDB; Q01757; -.
DR   SMR; Q01757; -.
DR   STRING; 443255.SCLAV_4200; -.
DR   UniPathway; UPA00149; UER00239.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050564; F:N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; ATP-binding; Ligase; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphopantetheine; Repeat.
FT   CHAIN           1..>805
FT                   /note="N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine
FT                   synthase"
FT                   /id="PRO_0000193062"
FT   REGION          783..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         805
SQ   SEQUENCE   805 AA;  88718 MW;  2171303A98C7CA36 CRC64;
     MMSARYPRTA AEWTTRIQGV SSERCDLEML LKDEWRNRIA VRDDDPGVRA TRQRDIVVDG
     REYTALKDAL RAADGVSAGA LALASLHSVM RAYGHGEQTV AAFVDATATA ELKTAAVLPV
     IVDHIEHTRL TCAEAIRELD ETLRRKDSYT RADEVLQRGL FDALLVLAER EVALSELPSA
     PLVMVVRDDA ARGRLCWTMA YAGELFEDTT VAGVLEVVRE VLGQYAGRPG DRVAEIELAS
     REQRERLQRW NATDGDFPAD QRLNDLVEAA VRRSPDREAV VFGTQRLTYR EVDARANRFA
     HWLLGPGLGV RSQQLVGIFL DKSDLGVVAT LGIWKAGAAY VPIDPAYPAE RVRFAVGDTG
     LRGIVTNRHH AGRLREILGA EHADVTVVEI ESVLDEQAAA DTDGLLSVKP ELALGVRDLA
     YLTYTSGTTG VPKGVPKYHD SVVNSITDLS ERYDMRRPGT ERVALFASYV FEPHLRQTLI
     ALINGQTLVV VPEEVRLDPD RFPAYIEEHG VTYLNATGSV LQHFDLRRRT SLKRLLLVGE
     ELTAAGLRQL RERFSGRIVN EYAFTEAAFV TAVKKFAPGV TERADRSIGR PVRNVKWYVL
     SQDLKRLPVG AIGELYIGGC GVAPGYLNRD DLTAERFLTN PYASEQDRAR GTNARIYRTG
     DLARMLPSGE VEFMGRSDFQ LKLNGVRVEP GEIEAQATEY AGVRKCVVIA REGAGGGSDR
     HLVGYYLTEP GAGVTEAELL SFLERRLIRI MVPARMVRLE SIPVNVNGKV DWRALPEVDL
     ARPDTGGGAV GSTTTGGVRG ELREI