DESV_STRVZ
ID DESV_STRVZ Reviewed; 379 AA.
AC Q9ZGH4;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose transaminase {ECO:0000303|PubMed:17456741};
DE EC=2.6.1.106 {ECO:0000303|PubMed:17456741};
GN Name=desV {ECO:0000303|PubMed:17456741};
OS Streptomyces venezuelae.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=54571;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15439 / DSM 41110 / IMRU3627 / M-2140;
RX PubMed=9770448; DOI=10.1073/pnas.95.21.12111;
RA Xue Y., Zhao L., Liu H.W., Sherman D.H.;
RT "A gene cluster for macrolide antibiotic biosynthesis in Streptomyces
RT venezuelae: architecture of metabolic diversity.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12111-12116(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP ANALOG, FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 15439 / DSM 41110 / IMRU3627 / M-2140;
RX PubMed=17456741; DOI=10.1110/ps.062711007;
RA Burgie E.S., Thoden J.B., Holden H.M.;
RT "Molecular architecture of DesV from Streptomyces venezuelae: a PLP-
RT dependent transaminase involved in the biosynthesis of the unusual sugar
RT desosamine.";
RL Protein Sci. 16:887-896(2007).
CC -!- FUNCTION: Involved in the biosynthesis of dTDP-alpha-D-desosamine, a
CC sugar found in several bacterial macrolide antibiotics. Catalyzes the
CC reversible transfer of the amino group from L-glutamate to the C-3
CC position of dTDP-3-keto-4,6-deoxyglucose to yield dTDP-3-amino-3,4,6-
CC trideoxyglucose. {ECO:0000305|PubMed:17456741}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose =
CC dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucose + L-glutamate;
CC Xref=Rhea:RHEA:39907, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:63262, ChEBI:CHEBI:76280; EC=2.6.1.106;
CC Evidence={ECO:0000305|PubMed:17456741};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:17456741};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17456741}.
CC -!- SIMILARITY: Belongs to the degT/dnrJ/eryC1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF079762; AAC68680.1; -; Genomic_DNA.
DR RefSeq; WP_055641633.1; NZ_CP013129.1.
DR PDB; 2OGA; X-ray; 2.05 A; A/B/C/D=1-379.
DR PDB; 2OGE; X-ray; 2.05 A; A/B/C/D=1-379.
DR PDBsum; 2OGA; -.
DR PDBsum; 2OGE; -.
DR AlphaFoldDB; Q9ZGH4; -.
DR SMR; Q9ZGH4; -.
DR KEGG; ag:AAC68680; -.
DR OrthoDB; 1006364at2; -.
DR BioCyc; MetaCyc:MON-16953; -.
DR BRENDA; 2.6.1.106; 6106.
DR EvolutionaryTrace; Q9ZGH4; -.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
DR GO; GO:0033068; P:macrolide biosynthetic process; IDA:UniProtKB.
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; Antibiotic biosynthesis; Pyridoxal phosphate; Transferase.
FT CHAIN 1..379
FT /note="dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose
FT transaminase"
FT /id="PRO_0000430832"
FT BINDING 67
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17456741"
FT BINDING 167
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17456741"
FT BINDING 188..193
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17456741"
FT BINDING 221
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17456741"
FT BINDING 227
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17456741"
FT BINDING 235..237
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17456741"
FT BINDING 318
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17456741"
FT MOD_RES 193
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305|PubMed:17456741"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:2OGA"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:2OGA"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:2OGA"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:2OGA"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:2OGA"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 121..127
FT /evidence="ECO:0007829|PDB:2OGA"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:2OGA"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2OGE"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:2OGA"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2OGA"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 253..270
FT /evidence="ECO:0007829|PDB:2OGA"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:2OGA"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 339..347
FT /evidence="ECO:0007829|PDB:2OGA"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:2OGA"
FT HELIX 359..374
FT /evidence="ECO:0007829|PDB:2OGA"
SQ SEQUENCE 379 AA; 41184 MW; 1A4FD0F4E76DCCDB CRC64;
MSSRAETPRV PFLDLKAAYE ELRAETDAAI ARVLDSGRYL LGPELEGFEA EFAAYCETDH
AVGVNSGMDA LQLALRGLGI GPGDEVIVPS HTYIASWLAV SATGATPVPV EPHEDHPTLD
PLLVEKAITP RTRALLPVHL YGHPADMDAL RELADRHGLH IVEDAAQAHG ARYRGRRIGA
GSSVAAFSFY PGKNLGCFGD GGAVVTGDPE LAERLRMLRN YGSRQKYSHE TKGTNSRLDE
MQAAVLRIRL AHLDSWNGRR SALAAEYLSG LAGLPGIGLP VTAPDTDPVW HLFTVRTERR
DELRSHLDAR GIDTLTHYPV PVHLSPAYAG EAPPEGSLPR AESFARQVLS LPIGPHLERP
QALRVIDAVR EWAERVDQA
