MEDII_MICMH
ID MEDII_MICMH Reviewed; 374 AA.
AC Q9F837;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose transaminase {ECO:0000303|PubMed:20418422};
DE EC=2.6.1.106 {ECO:0000269|PubMed:20418422};
GN Name=megDII {ECO:0000303|PubMed:20418422};
OS Micromonospora megalomicea subsp. nigra.
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Micromonospora.
OX NCBI_TaxID=136926;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 27598 / DSM 802 / NBRC 14744 / NCIMB 12662 / NRRL 3275;
RX PubMed=10972798; DOI=10.1046/j.1365-2958.2000.02059.x;
RA Volchegursky Y., Hu Z., Katz L., McDaniel R.;
RT "Biosynthesis of the anti-parasitic agent megalomicin: transformation of
RT erythromycin to megalomicin in Saccharopolyspora erythraea.";
RL Mol. Microbiol. 37:752-762(2000).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 27598 / DSM 802 / NBRC 14744 / NCIMB 12662 / NRRL 3275;
RX PubMed=16514147; DOI=10.1099/mic.0.28680-0;
RA Rodriguez E., Peiru S., Carney J.R., Gramajo H.;
RT "In vivo characterization of the dTDP-D-desosamine pathway of the
RT megalomicin gene cluster from Micromonospora megalomicea.";
RL Microbiology 152:667-673(2006).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 27598 / DSM 802 / NBRC 14744 / NCIMB 12662 / NRRL 3275;
RX PubMed=20418422; DOI=10.1128/aem.03083-09;
RA Useglio M., Peiru S., Rodriguez E., Labadie G.R., Carney J.R., Gramajo H.;
RT "TDP-L-megosamine biosynthesis pathway elucidation and megalomicin a
RT production in Escherichia coli.";
RL Appl. Environ. Microbiol. 76:3869-3877(2010).
CC -!- FUNCTION: Involved in the biosynthesis of the amino sugar dTDP-L-
CC megosamine which is found in the macrolide antibiotic and antiparasitic
CC megalomicin A. Catalyzes the reversible transfer of the amino group
CC from L-glutamate to the C-3 position of dTDP-3-keto-4,6-deoxyglucose to
CC yield dTDP-3-amino-3,4,6-trideoxyglucose. {ECO:0000269|PubMed:10972798,
CC ECO:0000269|PubMed:16514147, ECO:0000269|PubMed:20418422}.
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:0000269|PubMed:20418422};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q9ZGH4};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the degT/dnrJ/eryC1 family. {ECO:0000305}.
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DR EMBL; AF263245; AAG13910.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9F837; -.
DR SMR; Q9F837; -.
DR KEGG; ag:AAG13910; -.
DR BioCyc; MetaCyc:MON-17629; -.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS: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 Antibiotic biosynthesis; Pyridoxal phosphate; Transferase.
FT CHAIN 1..374
FT /note="dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose
FT transaminase"
FT /id="PRO_0000430833"
FT BINDING 60
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9ZGH4"
FT BINDING 160
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9ZGH4"
FT BINDING 181..186
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9ZGH4"
FT BINDING 214
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9ZGH4"
FT BINDING 221
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9ZGH4"
FT BINDING 229..231
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9ZGH4"
FT BINDING 316
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9ZGH4"
FT MOD_RES 186
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ZGH4"
SQ SEQUENCE 374 AA; 41521 MW; 82356AFBC98BD3E1 CRC64;
MTTYVWSYLL EYERERADIL DAVQKVFASG SLILGQSVEN FETEYARYHG IAHCVGVDNG
TNAVKLALES VGVGRDDEVV TVSNTAAPTV LAIDEIGARP VFVDVRDEDY LMDTDLVEAA
VTPRTKAIVP VHLYGQCVDM TALRELADRR GLKLVEDCAQ AHGARRDGRL AGTMSDAAAF
SFYPTKVLGA YGDGGAVVTN DDETARALRR LRYYGMEEVY YVTRTPGHNS RLDEVQAEIL
RRKLTRLDAY VAGRRAVAQR YVDGLADLQD SHGLELPVVT DGNEHVFYVY VVRHPRRDEI
IKRLRDGYDI SLNISYPWPV HTMTGFAHLG VASGSLPVTE RLAGEIFSLP MYPSLPHDLQ
DRVIEAVREV ITGL
