GLDSA_NIACI
ID GLDSA_NIACI Reviewed; 418 AA.
AC Q8G8Y2;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=L-glutamine:2-deoxy-scyllo-inosose aminotransferase;
DE Short=L-glutamine:DOI aminotransferase;
DE EC=2.6.1.100 {ECO:0000269|PubMed:12374384, ECO:0000269|PubMed:12478783, ECO:0000269|PubMed:15839685};
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:0000269|PubMed:12374384, ECO:0000269|PubMed:12478783, ECO:0000269|PubMed:15839685};
GN Name=btrR; Synonyms=btrS;
OS Niallia circulans (Bacillus circulans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=1397;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12478783; DOI=10.1039/b209799k;
RA Huang F., Li Y., Yu J., Spencer J.B.;
RT "Biosynthesis of aminoglycoside antibiotics: cloning, expression and
RT characterisation of an aminotransferase involved in the pathway to 2-
RT deoxystreptamine.";
RL Chem. Commun. (Camb.) 23:2860-2861(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=SANK 72073;
RX PubMed=12374384; DOI=10.7164/antibiotics.55.707;
RA Tamegai H., Nango E., Kuwahara M., Yamamoto H., Ota Y., Kuriki H.,
RA Eguchi T., Kakinuma K.;
RT "Identification of L-glutamine: 2-deoxy-scyllo-inosose aminotransferase
RT required for the biosynthesis of butirosin in Bacillus circulans.";
RL J. Antibiot. 55:707-714(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION STEREOCHEMISTRY.
RC STRAIN=SANK 72073;
RX PubMed=15839685; DOI=10.1021/ja0445948;
RA Yokoyama K., Kudo F., Kuwahara M., Inomata K., Tamegai H., Eguchi T.,
RA Kakinuma K.;
RT "Stereochemical recognition of doubly functional aminotransferase in 2-
RT deoxystreptamine biosynthesis.";
RL J. Am. Chem. Soc. 127:5869-5874(2005).
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:0000269|PubMed:12374384, ECO:0000269|PubMed:12478783,
CC ECO:0000269|PubMed:15839685}.
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:0000269|PubMed:12374384, ECO:0000269|PubMed:12478783,
CC ECO:0000269|PubMed:15839685};
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:0000269|PubMed:12374384, ECO:0000269|PubMed:12478783,
CC ECO:0000269|PubMed:15839685};
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: Metabolic intermediate biosynthesis; 2-deoxystreptamine
CC biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 4/4.
CC -!- PATHWAY: Antibiotic biosynthesis; butirosin 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; AJ494863; CAD41947.1; -; Genomic_DNA.
DR EMBL; AB097196; BAE07061.1; -; Genomic_DNA.
DR PDB; 2C7T; X-ray; 2.10 A; A=1-418.
DR PDB; 2C81; X-ray; 1.70 A; A=1-418.
DR PDB; 5W71; X-ray; 2.10 A; A/B=1-418.
DR PDBsum; 2C7T; -.
DR PDBsum; 2C81; -.
DR PDBsum; 5W71; -.
DR AlphaFoldDB; Q8G8Y2; -.
DR SMR; Q8G8Y2; -.
DR PRIDE; Q8G8Y2; -.
DR KEGG; ag:BAE07061; -.
DR BioCyc; MetaCyc:MON-17229; -.
DR BRENDA; 2.6.1.100; 649.
DR BRENDA; 2.6.1.101; 649.
DR UniPathway; UPA00907; UER00922.
DR UniPathway; UPA00907; UER00924.
DR UniPathway; UPA00964; -.
DR EvolutionaryTrace; Q8G8Y2; -.
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 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Antibiotic biosynthesis;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..418
FT /note="L-glutamine:2-deoxy-scyllo-inosose aminotransferase"
FT /id="PRO_0000233016"
FT MOD_RES 192
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:2C81"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 265..283
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:2C81"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 320..331
FT /evidence="ECO:0007829|PDB:2C81"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 367..371
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 376..384
FT /evidence="ECO:0007829|PDB:2C81"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:2C81"
FT HELIX 397..412
FT /evidence="ECO:0007829|PDB:2C81"
SQ SEQUENCE 418 AA; 47032 MW; 41E7C1102D36D289 CRC64;
MTIPFDHWPE WPQHSDRTRR KIEEVFQSNR WAISGYWTGE ESMERKFAKA FADFNGVPYC
VPTTSGSTAL MLALEALGIG EGDEVIVPSL TWIATATAVL NVNALPVFVD VEADTYCIDP
QLIKSAITDK TKAIIPVHLF GSMANMDEIN EIAQEHNLFV IEDCAQSHGS VWNNQRAGTI
GDIGAFSCQQ GKVLTAGEGG IIVTKNPRLF ELIQQLRADS RVYCDDSSEL MHGDMQLVKK
GDIQGSNYCL SEFQSAILLD QLQELDDKNA IREKNAMFLN DALSKIDGIK VMKRPPQVSR
QTYYGYVFRF DPVKFGGLNA DQFCEILREK LNMGTFYLHP PYLPVHKNPL FCPWTKNRYL
KSVRKTEAYW RGLHYPVSER ASGQSIVIHH AILLAEPSHL SLLVDAVAEL ARKFCVTH
