ID   CAMYS_STRVI             Reviewed;         389 AA.
AC   Q84CG1;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Capreomycidine synthase;
DE            EC=4.2.1.145 {ECO:0000269|PubMed:15368581, ECO:0000269|PubMed:15368582};
DE   AltName: Full=Viomycin biosynthesis protein C;
GN   Name=vioD {ECO:0000303|PubMed:12936980};
GN   Synonyms=svaT {ECO:0000312|EMBL:AAO66428.1};
OS   Streptomyces vinaceus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11861;
RX   PubMed=12936980; DOI=10.1128/aac.47.9.2823-2830.2003;
RA   Thomas M.G., Chan Y.A., Ozanick S.G.;
RT   "Deciphering tuberactinomycin biosynthesis: isolation, sequencing, and
RT   annotation of the viomycin biosynthetic gene cluster.";
RL   Antimicrob. Agents Chemother. 47:2823-2830(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11861;
RX   PubMed=12909358; DOI=10.1016/s0378-1119(03)00617-6;
RA   Yin X., O'Hare T., Gould S.J., Zabriskie T.M.;
RT   "Identification and cloning of genes encoding viomycin biosynthesis from
RT   Streptomyces vinaceus and evidence for involvement of a rare oxygenase.";
RL   Gene 312:215-224(2003).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 11861;
RX   PubMed=15368581; DOI=10.1002/cbic.200400187;
RA   Yin X., McPhail K.L., Kim K.J., Zabriskie T.M.;
RT   "Formation of the nonproteinogenic amino acid 2S,3R-capreomycidine by VioD
RT   from the viomycin biosynthesis pathway.";
RL   ChemBioChem 5:1278-1281(2004).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 11861;
RX   PubMed=15368582; DOI=10.1002/cbic.200400136;
RA   Ju J., Ozanick S.G., Shen B., Thomas M.G.;
RT   "Conversion of (2S)-arginine to (2S,3R)-capreomycidine by VioC and VioD
RT   from the viomycin biosynthetic pathway of Streptomyces sp. strain ATCC
RT   11861.";
RL   ChemBioChem 5:1281-1285(2004).
CC   -!- FUNCTION: Involved in the biosynthesis of capreomycidine, an unusual
CC       amino acid used by non-ribosomal peptide synthases (NRPS) to make the
CC       tuberactinomycin class of peptide antibiotic such as viomycin and
CC       capreomycin. Catalyzes the dehydration of the C3 hydroxyl of (3S)-
CC       hydroxy-(2S)-arginine and the intramolecular cyclization to yield
CC       (2S,3R)-capreomycidine. {ECO:0000269|PubMed:15368581,
CC       ECO:0000269|PubMed:15368582}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3S)-hydroxyarginine = (2S,3R)-capreomycidine + H2O;
CC         Xref=Rhea:RHEA:38159, ChEBI:CHEBI:15377, ChEBI:CHEBI:73938,
CC         ChEBI:CHEBI:75665; EC=4.2.1.145;
CC         Evidence={ECO:0000269|PubMed:15368581, ECO:0000269|PubMed:15368582};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P12998};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:15368581,
CC       ECO:0000269|PubMed:15368582}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AY225601; AAO66428.1; -; Genomic_DNA.
DR   EMBL; AY263398; AAP92494.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q84CG1; -.
DR   SMR; Q84CG1; -.
DR   PRIDE; Q84CG1; -.
DR   KEGG; ag:AAP92494; -.
DR   GO; GO:0016842; F:amidine-lyase activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR023965; Capreomycidine_synthase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03947; viomycin_VioD; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..389
FT                   /note="Capreomycidine synthase"
FT                   /id="PRO_0000424866"
FT   MOD_RES         230
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P12998"
SQ   SEQUENCE   389 AA;  42049 MW;  371BD92EA60B3161 CRC64;
     MTGPLGAGPQ ALPAAPLEDW LRERYFQAKT DISSSGVHNY TFGELRALDP ALLGTRELDQ
     LMFRDGPSLG DERLRAAVAA RVRPGPGHVV MTTHGSSEAL YLAFAALVRP GDEVVVATPA
     YHSLSGLATA AGASLRPWPL RPENGFAPDL DDLRAVLSDR TRLVVVNFPH NPSGACVDPR
     GRTELLDLVA NSQAVLLWDG AFTDLVHDHP PLAEPSQDLD RVLSFGTLSK AYGLPGLRVG
     WCVVPQDLVS ELVRIRDYLT LSLSPLVERV AAVAVEHADA LITPRLTEAR HNRRRVLEWA
     AASEGAIDCP VPRGGVTAFP RFTAHTDVTD LCERLLARHG VLVVPGRVFG QADRMRIGFS
     CPRPELERGL AAISEELGTH ARGRRRGTG