ID   BTRB_NIACI              Reviewed;         432 AA.
AC   Q4H4F5;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Neamine transaminase BtrB;
DE            EC=2.6.1.93;
DE   AltName: Full=Butirosin biosynthesis protein B;
GN   Name=btrB;
OS   Niallia circulans (Bacillus circulans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=1397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21557 / NCIMB 12336 / BU-1709-YQW-B6;
RX   PubMed=16156513; DOI=10.1038/ja.2005.47;
RA   Kudo F., Numakura M., Tamegai H., Yamamoto H., Eguchi T., Kakinuma K.;
RT   "Extended sequence and functional analysis of the butirosin biosynthetic
RT   gene cluster in Bacillus circulans SANK 72073.";
RL   J. Antibiot. 58:373-379(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21557 / NCIMB 12336 / BU-1709-YQW-B6;
RA   Aboshanab K.M., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA   Piepersberg W.;
RT   "Analysis and comparison of the biosynthetic gene clusters for the 2-
RT   deoxystreptamine-containing aminoglycoside antibiotics ribostamycin,
RT   neomycin, lividomycin, paromomycin and butirosin.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 21557 / NCIMB 12336 / BU-1709-YQW-B6;
RX   PubMed=17206729; DOI=10.1002/cbic.200600371;
RA   Huang F., Spiteller D., Koorbanally N.A., Li Y., Llewellyn N.M.,
RA   Spencer J.B.;
RT   "Elaboration of neosamine rings in the biosynthesis of neomycin and
RT   butirosin.";
RL   ChemBioChem 8:283-288(2007).
CC   -!- FUNCTION: 6'-oxoglucosaminyl:L-glutamate aminotransferase that
CC       catalyzes pyridoxal-5'-phosphate-mediated transamination for the
CC       conversion of paromamine to neamine in the biosynthetic pathway of
CC       butirosin. {ECO:0000269|PubMed:17206729}.
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:17206729};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Antibiotic biosynthesis; butirosin biosynthesis.
CC       {ECO:0000269|PubMed:17206729}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AB097196; BAE07066.1; -; Genomic_DNA.
DR   EMBL; AJ781030; CAG77420.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4H4F5; -.
DR   SMR; Q4H4F5; -.
DR   PRIDE; Q4H4F5; -.
DR   KEGG; ag:BAE07066; -.
DR   BioCyc; MetaCyc:MON-17279; -.
DR   UniPathway; UPA00964; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
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; 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; 2.
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..432
FT                   /note="Neamine transaminase BtrB"
FT                   /id="PRO_0000421734"
FT   MOD_RES         245
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   432 AA;  48380 MW;  1EE9C0E9A7300F1D CRC64;
     MKQETVKSSE QLLSVLGTYI DSPVDPFRKE RVMFSRGSGA YLFDYDGGNY IDLMNGKGSI
     ILGHNDPSVN AALRNFLEQD REVVTGPSKP IIDLAERIKK DSALPDAKVS FYTTGTAACR
     AAVYAARDYS GKKIVLSSGY HGWDPMWRQQ GPLLEPNEDG VIEFYFIPEL LERALTAHKD
     QVALVIFSPD YTYLSASTME RILGICRAHG VLVCCDDVKQ GYRHRQGSSL ELVTTEKADM
     YVFSKGLSNG HRISCVVSSD EIMAETKEHT YTAYYQMLPI LSSLETLKKM ESGKGYDLIR
     SYGQTLTGNL KELFVQSSLP IEVNGSSIFQ LVFGDEELEE AFYREAFIQG LILFEGDNQS
     LSLCMDKDVQ VDLIRRFANV TDVLSEQFKH LRGKEVTTEQ TFRTAWNMID GASDLLPYEK
     QLKLLDNLIG GG