ID   KACL_STRKN              Reviewed;         392 AA.
AC   Q6L741;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=2'-deamino-2'-hydroxyneamine transaminase;
DE            EC=2.6.1.94 {ECO:0000269|PubMed:21983602};
DE   AltName: Full=Kanamycin biosynthesis protein B;
DE   AltName: Full=Neamine transaminase KanB;
DE            EC=2.6.1.93 {ECO:0000269|PubMed:21983602};
GN   Name=kacL; Synonyms=kanB;
OS   Streptomyces kanamyceticus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM
RC   Ac-837;
RX   PubMed=15313224; DOI=10.1016/j.abb.2004.06.009;
RA   Kharel M.K., Subba B., Basnet D.B., Woo J.S., Lee H.C., Liou K.,
RA   Sohng J.K.;
RT   "A gene cluster for biosynthesis of kanamycin from Streptomyces
RT   kanamyceticus: comparison with gentamicin biosynthetic gene cluster.";
RL   Arch. Biochem. Biophys. 429:204-214(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15303497; DOI=10.7164/antibiotics.57.351;
RA   Yanai K., Murakami T.;
RT   "The kanamycin biosynthetic gene cluster from Streptomyces kanamyceticus.";
RL   J. Antibiot. 57:351-354(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM
RC   Ac-837;
RA   Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA   Piepersberg W.;
RT   "Cloning and sequencing of the kanamycin biosynthetic gene cluster from
RT   Streptomyces kanamyceticus DSM 40500.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=21983602; DOI=10.1038/nchembio.671;
RA   Park J.W., Park S.R., Nepal K.K., Han A.R., Ban Y.H., Yoo Y.J., Kim E.J.,
RA   Kim E.M., Kim D., Sohng J.K., Yoon Y.J.;
RT   "Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic
RT   manipulation.";
RL   Nat. Chem. Biol. 7:843-852(2011).
CC   -!- FUNCTION: Aminotransferase that has 6'-oxoglucosaminyl:L-glutamate
CC       aminotransferase activity by catalyzing pyridoxal-5'-phosphate-mediated
CC       transamination leading to the conversion of paromamine to neamine in
CC       the biosynthetic pathway of kanamycin B. {ECO:0000269|PubMed:21983602}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + neamine = 6'-oxoparomamine + L-glutamate;
CC         Xref=Rhea:RHEA:34039, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:65016, ChEBI:CHEBI:65076; EC=2.6.1.93;
CC         Evidence={ECO:0000269|PubMed:21983602};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deamino-2'-hydroxyneamine + 2-oxoglutarate = 2'-deamino-2'-
CC         hydroxy-6'-dehydroparomamine + L-glutamate; Xref=Rhea:RHEA:34299,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:67213,
CC         ChEBI:CHEBI:67214; EC=2.6.1.94;
CC         Evidence={ECO:0000269|PubMed:21983602};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Antibiotic biosynthesis; kanamycin biosynthesis.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AJ582817; CAF60533.1; -; Genomic_DNA.
DR   EMBL; AB164642; BAD20756.1; -; Genomic_DNA.
DR   EMBL; AJ628422; CAF31586.1; -; Genomic_DNA.
DR   RefSeq; WP_055545102.1; NZ_LIQU01000069.1.
DR   AlphaFoldDB; Q6L741; -.
DR   SMR; Q6L741; -.
DR   KEGG; ag:CAF60533; -.
DR   BioCyc; MetaCyc:MON-17221; -.
DR   UniPathway; UPA00965; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
DR   GO; GO:1901133; P:kanamycin biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Antibiotic biosynthesis; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..392
FT                   /note="2'-deamino-2'-hydroxyneamine transaminase"
FT                   /id="PRO_0000421733"
FT   MOD_RES         249
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   392 AA;  43095 MW;  2DA9009195D315AB CRC64;
     MSTHPVLDWS RSAEHLRRSH GVTTDPRPDE DGHYPCVLTR GSGTRVYDLD GNAYLDLTGS
     FGSVLIGHAE PAVVRAVTDV LSEGNLFYTG ASPRRLALAE RLLDWFPWSE QAIFYRTGSC
     AVSAAARLAQ HATGRNRVLS SGYHGWHDWH LEAVPEAKPK TFESYATEFH NDLALYRSWL
     DRHGEEIAAV VVTPEPHRFD HAYYQELREV AKEHGCLFVV DEVKTGFRAG AGGFSALAGI
     EPDAVTVSKG MANGHSISAV VGQRQLTQEL SEAHVWSTYQ NEQVGFAAAL ASLDFLERHD
     VAAVTRRTGE AVRQGVLQLF AEHGLPVGAP GWGPMFELDF DAADEGLAER LEAALLRHGI
     FCDTGDDFNM MFHTAEHTDE LLERFAAALG DL