SPNR_SACSN
ID SPNR_SACSN Reviewed; 385 AA.
AC Q9ALN9;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=dTDP-4-dehydro-2,3,6-trideoxy-D-glucose 4-aminotransferase {ECO:0000303|PubMed:18345667};
DE EC=2.6.1.110 {ECO:0000269|PubMed:18345667};
DE AltName: Full=dTDP-4-keto-2,3,6-trideoxy-D-glucose 4-aminotransferase {ECO:0000303|PubMed:18345667};
GN Name=spnR {ECO:0000303|PubMed:11358695};
OS Saccharopolyspora spinosa.
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharopolyspora.
OX NCBI_TaxID=60894;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=11358695; DOI=10.1016/s1074-5521(01)00029-1;
RA Waldron C., Matsushima P., Rosteck P.R. Jr., Broughton M.C., Turner J.,
RA Madduri K., Crawford K.P., Merlo D.J., Baltz R.H.;
RT "Cloning and analysis of the spinosad biosynthetic gene cluster of
RT Saccharopolyspora spinosa.";
RL Chem. Biol. 8:487-499(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=NRRL 18537;
RX PubMed=18345667; DOI=10.1021/ja0771383;
RA Hong L., Zhao Z., Melancon C.E. III, Zhang H., Liu H.W.;
RT "In vitro characterization of the enzymes involved in TDP-D-forosamine
RT biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa.";
RL J. Am. Chem. Soc. 130:4954-4967(2008).
CC -!- FUNCTION: Involved in the biosynthesis of forosamine ((4-
CC dimethylamino)-2,3,4,6-tetradeoxy-alpha-D-threo-hexopyranose), a highly
CC deoxygenated sugar component of several bioactive natural products such
CC as the insecticidal spinosyns A and D (PubMed:11358695,
CC PubMed:18345667). In the presence of pyridoxal 5'-phosphate (PLP) and
CC alpha-ketoglutarate, catalyzes the C-4 transamination of dTDP-4-keto-
CC 2,3,6-trideoxy-alpha-D-glucose to yield dTDP-4-amino-2,3,4,6-
CC tetradeoxy-alpha-D-glucose (PubMed:18345667). It can also use pyruvate,
CC but less efficiently than alpha-ketoglutarate (PubMed:18345667). Also
CC able to catalyze the C-4 transamination of dTDP-4-keto-2,6-dideoxy-
CC alpha-D-glucose to yield dTDP-4-amino-2,4,6-trideoxy-D-glucose
CC (PubMed:18345667). {ECO:0000269|PubMed:11358695,
CC ECO:0000269|PubMed:18345667}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + dTDP-4-amino-2,3,4,6-tetradeoxy-alpha-D-
CC erythro-hexopyranose = dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-
CC hexopyranose + L-glutamate; Xref=Rhea:RHEA:49144, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:90944, ChEBI:CHEBI:90945;
CC EC=2.6.1.110; Evidence={ECO:0000269|PubMed:18345667};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:18345667};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18345667}.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
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DR EMBL; AY007564; AAG23279.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ALN9; -.
DR SMR; Q9ALN9; -.
DR STRING; 994479.GL877879_gene4838; -.
DR KEGG; ag:AAG23279; -.
DR BioCyc; MetaCyc:MON-16622; -.
DR BRENDA; 2.6.1.110; 13744.
DR GO; GO:0008483; F:transaminase activity; 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 Aminotransferase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..385
FT /note="dTDP-4-dehydro-2,3,6-trideoxy-D-glucose 4-
FT aminotransferase"
FT /id="PRO_0000444372"
FT MOD_RES 182
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:A8GDR5"
SQ SEQUENCE 385 AA; 42296 MW; 84DF30621E18B58E CRC64;
MINLHQPILG TEELDAIAEV FASNWIGLGP RTRTFEAEFA HHLGVDPEQV VFLNSGTAAL
FLTVQVLDLG PGDDVVLPSI SFVAAANAIA SSGARPVFCD VDPRTLNPTL DDVARAITPA
TKAVLLLHYG GSPGEVTAIA DFCREKGLML IEDSACAVAS SVHGTACGTF GDLATWSFDA
MKILVTGDGG MFYAADPELA HRARRLAYHG LEQMSGFDSA KSSNRWWDIR VEDIGQRLIG
NDMTAALGSV QLRKLPEFIN RRREIATQYD RLLSDVPGVL LPPTLPDGHV SSHYFYWVQL
APEIRDQVAQ QMLERGIYTS YRYPPLHKVP IYRADCKLPS AEDACRRTLL LPLHPSLDDA
EVRTVADEFQ KAVEHHISQR SPLRK
