GLDSA_MICEC
ID GLDSA_MICEC Reviewed; 420 AA.
AC Q6QVU4; Q70KC9;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=L-glutamine:2-deoxy-scyllo-inosose aminotransferase;
DE Short=L-glutamine:DOI aminotransferase;
DE EC=2.6.1.100 {ECO:0000250|UniProtKB:Q6L739};
DE AltName: Full=L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase;
DE Short=L-glutamine:amino-DOI aminotransferase;
DE EC=2.6.1.101 {ECO:0000250|UniProtKB:Q6L739};
GN Name=gntA; Synonyms=genS1, gtmB;
OS Micromonospora echinospora (Micromonospora purpurea).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Micromonospora.
OX NCBI_TaxID=1877;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15835 / DSM 43036 / BCRC 11561 / JCM 3074 / NBRC 12575 / NCIMB
RC 12882 / NRRL 2953;
RX PubMed=15376556; DOI=10.7164/antibiotics.57.436;
RA Unwin J., Standage S., Alexander D., Hosted T. Jr., Horan A.C.,
RA Wellington E.M.;
RT "Gene cluster in Micromonospora echinospora ATCC15835 for the biosynthesis
RT of the gentamicin C complex.";
RL J. Antibiot. 57:436-445(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15835 / DSM 43036 / BCRC 11561 / JCM 3074 / NBRC 12575 / NCIMB
RC 12882 / NRRL 2953;
RX PubMed=15359126;
RA Kharel M.K., Basnet D.B., Lee H.C., Liou K., Moon Y.H., Kim J.-J.,
RA Woo J.S., Sohng J.K.;
RT "Molecular cloning and characterization of a 2-deoxystreptamine
RT biosynthetic gene cluster in gentamicin-producing Micromonospora
RT echinospora ATCC15835.";
RL Mol. Cells 18:71-78(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15835 / DSM 43036 / BCRC 11561 / JCM 3074 / NBRC 12575 / NCIMB
RC 12882 / NRRL 2953;
RA Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA Piepersberg W.;
RT "Cloning and sequencing of the gentamicin biosynthetic gene cluster from
RT Micromonospora echinospora DSM 43036.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the PLP-dependent transamination of 2-deoxy-scyllo-
CC inosose (2-DOI) to form 2-deoxy-scyllo-inosamine (2-DOIA) using L-
CC glutamine as the amino donor. Also catalyzes the transamination of 3-
CC amino-2,3-dideoxy-scyllo-inosose (keto-2-DOIA) into 2-deoxystreptamine
CC (2-DOS). {ECO:0000250|UniProtKB:Q6L739}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-deoxy-L-scyllo-inosose + L-glutamine = 2-deoxy-scyllo-
CC inosamine + 2-oxoglutaramate; Xref=Rhea:RHEA:34147,
CC ChEBI:CHEBI:16769, ChEBI:CHEBI:58359, ChEBI:CHEBI:64796,
CC ChEBI:CHEBI:65003; EC=2.6.1.100;
CC Evidence={ECO:0000250|UniProtKB:Q6L739};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-amino-2,3-dideoxy-scyllo-inosose + L-glutamine = 2-
CC deoxystreptamine + 2-oxoglutaramate; Xref=Rhea:RHEA:34151,
CC ChEBI:CHEBI:16769, ChEBI:CHEBI:58359, ChEBI:CHEBI:65002,
CC ChEBI:CHEBI:65069; EC=2.6.1.101;
CC Evidence={ECO:0000250|UniProtKB:Q6L739};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 2-deoxystreptamine
CC biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 2/4.
CC -!- PATHWAY: Antibiotic biosynthesis; gentamicin biosynthesis.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. L-glutamine:2-deoxy-
CC scyllo-inosose/scyllo-inosose aminotransferase subfamily.
CC {ECO:0000305}.
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DR EMBL; AY524043; AAR98547.1; -; Genomic_DNA.
DR EMBL; AJ575934; CAE06512.2; -; Genomic_DNA.
DR EMBL; AJ628149; CAF31430.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6QVU4; -.
DR SMR; Q6QVU4; -.
DR UniPathway; UPA00907; UER00922.
DR UniPathway; UPA00967; -.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244; PTHR30244; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Antibiotic biosynthesis; Pyridoxal phosphate;
KW Transferase.
FT CHAIN 1..420
FT /note="L-glutamine:2-deoxy-scyllo-inosose aminotransferase"
FT /id="PRO_0000233017"
FT MOD_RES 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 420 AA; 44731 MW; 1C97AEEC7FE93DE7 CRC64;
MTLLAVNGGS PIRSQQWPLW PAPAPGALDA LNEVLHSGRW AISGPYQGKQ SFERRFAAAF
AEFHEIGHCV PTSSGTASLM VALEACGVGA GDEVIIPGLT WVANASTVAG VNAVPVPVDV
DPQTLCLDPA AVERAITPRT AAIVVVHLYS AVADLDALTA IAERHEIPLI EDCAQAHGAR
YRDRRVGTFG AFGTFSMQHS KVLTSGEGGA VITGDAALSR RAEHLRADGR TYTPDEPAVG
EMELAQTAEL MGSNRCLSEF QAALLLGQLE LLDEQNERRR ANAALLDEGL GALGIQPQVS
SPGTTERTYY EWAGRIEDDG IGQIGVERIA PAVAAELSGA AIYASYPPMN HNRLYQPATR
ARFKGIAGLD LTGYSLPVAE DAGQRVVTIH HSALLGDESD MKDIVRAFEK VFANHRELRG
