NEON_STRFR
ID NEON_STRFR Reviewed; 416 AA.
AC Q53U08;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Neamine transaminase NeoN;
DE EC=2.6.1.93;
DE AltName: Full=Glutamate--6'-dehydroparomamine aminotransferase;
DE AltName: Full=Neomycin C transaminase;
DE EC=2.6.1.95;
DE AltName: Full=Neomycin biosynthesis protein 18;
DE Short=Neo-18;
DE AltName: Full=Neomycin biosynthesis protein B;
DE AltName: Full=Neomycin biosynthesis protein N;
GN Name=neoN; Synonyms=neo18, neoB;
OS Streptomyces fradiae (Streptomyces roseoflavus).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1906;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC 8233 / NRRL B-1195 / VKM Ac-150;
RX PubMed=16506694; DOI=10.1038/ja.2005.104;
RA Kudo F., Yamamoto Y., Yokoyama K., Eguchi T., Kakinuma K.;
RT "Biosynthesis of 2-deoxystreptamine by three crucial enzymes in
RT Streptomyces fradiae NBRC 12773.";
RL J. Antibiot. 58:766-774(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC 8233 / NRRL B-1195 / VKM Ac-150;
RX PubMed=15827636; DOI=10.1039/b501199j;
RA Huang F., Haydock S.F., Mironenko T., Spiteller D., Li Y., Spencer J.B.;
RT "The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233:
RT characterisation of an aminotransferase involved in the formation of 2-
RT deoxystreptamine.";
RL Org. Biomol. Chem. 3:1410-1418(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC 8233 / NRRL B-1195 / VKM Ac-150;
RA Aboshanab K.M., Schmidt-Beissner H., Wehmeier U.F., Piepersberg W.,
RA Welzel K., Vente A.;
RT "Analysis and comparison of biosynthetic gene clusters for the 2-deoxy-
RT inosamine containing aminoglycoside antibiotics ribostamycin, neomycin,
RT lividomycin, paromomycin and butirosin.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RC STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC 8233 / NRRL B-1195 / VKM Ac-150;
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).
RN [5]
RP FUNCTION.
RX PubMed=21689223; DOI=10.1111/j.1365-2672.2011.05082.x;
RA Clausnitzer D., Piepersberg W., Wehmeier U.F.;
RT "The oxidoreductases LivQ and NeoQ are responsible for the different 6'-
RT modifications in the aminoglycosides lividomycin and neomycin.";
RL J. Appl. Microbiol. 111:642-651(2011).
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 neomycin. Also able to catalyze deamination at C-6''' of neomycin.
CC {ECO:0000269|PubMed:17206729, ECO:0000269|PubMed:21689223}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + neomycin C = 6'''-deamino-6'''-oxoneomycin C
CC + L-glutamate; Xref=Rhea:RHEA:33959, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:65068, ChEBI:CHEBI:65077; EC=2.6.1.95;
CC Evidence={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:0000269|PubMed:17206729};
CC -!- PATHWAY: Antibiotic biosynthesis; neomycin 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; AB211959; BAD95831.1; -; Genomic_DNA.
DR EMBL; AJ843080; CAH58701.1; -; Genomic_DNA.
DR EMBL; AJ629247; CAF33323.1; -; Genomic_DNA.
DR RefSeq; WP_031132478.1; NZ_MUNC01000397.1.
DR PDB; 6CBK; X-ray; 1.75 A; A/B/C/D=1-416.
DR PDB; 6CBL; X-ray; 1.60 A; A/B/C/D/E/F/G/H=1-416.
DR PDB; 6CBM; X-ray; 1.65 A; A/B=1-416.
DR PDB; 6CBN; X-ray; 1.35 A; A/B=1-416.
DR PDBsum; 6CBK; -.
DR PDBsum; 6CBL; -.
DR PDBsum; 6CBM; -.
DR PDBsum; 6CBN; -.
DR AlphaFoldDB; Q53U08; -.
DR SMR; Q53U08; -.
DR KEGG; ag:BAD95831; -.
DR BioCyc; MetaCyc:MON-17238; -.
DR UniPathway; UPA00969; -.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
DR GO; GO:1901158; P:neomycin 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.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Antibiotic biosynthesis;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..416
FT /note="Neamine transaminase NeoN"
FT /id="PRO_0000421735"
FT MOD_RES 231
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:6CBN"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:6CBN"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:6CBN"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:6CBN"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:6CBN"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:6CBN"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:6CBN"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:6CBN"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:6CBN"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:6CBN"
FT TURN 206..211
FT /evidence="ECO:0007829|PDB:6CBN"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:6CBN"
FT TURN 217..222
FT /evidence="ECO:0007829|PDB:6CBN"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:6CBN"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:6CBN"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 263..277
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 280..302
FT /evidence="ECO:0007829|PDB:6CBN"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:6CBN"
FT STRAND 313..322
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 323..335
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 354..370
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 382..393
FT /evidence="ECO:0007829|PDB:6CBN"
FT HELIX 403..413
FT /evidence="ECO:0007829|PDB:6CBN"
SQ SEQUENCE 416 AA; 44643 MW; 6771C74F7B2F5555 CRC64;
MTKNSSLLAE FPTCPRDEKD RPRVFTAASG AWLTDESGFR WIDFDNARGS ILLGHGDPVV
AEAVARAATG ADGTATGWSR RVDAVLERLH ALCGGEVVGL FRSGTAAVRA AVLAVREATG
RPLLLSAGYH GYDPMWYPSE APLEPNADGV VDFFFDLGLL RELLRAPERV AAVVVSPDHM
HLSPGWYREL RRLCSAAGVV LVADEVKVGL RYAPGLSTAE LLAPDVWVVA KGMANGHAVS
AVGGSRRLLK PLKEVSFTSF FEPTILAAAD AALARVATGE PQRAVREAGD RFLRHARKAL
DDASLPVEIA GDGTFFQFVP ATEELEEALY GAANAEGLLF YAGDNQGVSA AFDEAVLGEA
ERRFARVCER LAPYAGGEPV GDAARYRVAW NVMDGLRQAP RDREETTGLL ARLLDD
