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TGDS_MIMIV
ID   TGDS_MIMIV              Reviewed;         323 AA.
AC   Q5UR12;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Putative dTDP-D-glucose 4,6-dehydratase;
DE            EC=4.2.1.46;
GN   OrderedLocusNames=MIMI_R141;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose
CC         + H2O; Xref=Rhea:RHEA:17221, ChEBI:CHEBI:15377, ChEBI:CHEBI:57477,
CC         ChEBI:CHEBI:57649; EC=4.2.1.46;
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. dTDP-glucose dehydratase subfamily. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50416.1; -; Genomic_DNA.
DR   RefSeq; YP_003986633.1; NC_014649.1.
DR   PDB; 6VLO; X-ray; 2.05 A; A/B/C/D=1-323.
DR   PDBsum; 6VLO; -.
DR   SMR; Q5UR12; -.
DR   GeneID; 9924741; -.
DR   KEGG; vg:9924741; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
DR   CDD; cd05246; dTDP_GD_SDR_e; 1.
DR   InterPro; IPR005888; dTDP_Gluc_deHydtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Lyase; NAD; Reference proteome.
FT   CHAIN           1..323
FT                   /note="Putative dTDP-D-glucose 4,6-dehydratase"
FT                   /id="PRO_0000309205"
FT   ACT_SITE        125
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        126
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        149
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   TURN            8..10
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   HELIX           12..24
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   STRAND          29..34
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   STRAND          51..55
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   HELIX           61..70
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   STRAND          75..78
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   HELIX           91..99
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   HELIX           101..113
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   STRAND          117..124
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   STRAND          129..132
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   TURN            134..136
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   STRAND          139..143
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   HELIX           148..167
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   STRAND          171..176
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   STRAND          178..181
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   HELIX           189..198
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   STRAND          203..206
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   STRAND          212..217
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   HELIX           218..231
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   STRAND          237..240
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   STRAND          245..247
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   HELIX           248..259
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   TURN            264..266
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   STRAND          267..270
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   HELIX           285..289
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   HELIX           299..313
FT                   /evidence="ECO:0007829|PDB:6VLO"
FT   HELIX           314..316
FT                   /evidence="ECO:0007829|PDB:6VLO"
SQ   SEQUENCE   323 AA;  36874 MW;  A5289D45C9EF8D4B CRC64;
     MKNILVTGGL GFIGSNFVNH ISSKYDNVNI YVYDIGDYCA SVENVEWNNR TKLIKGDIRN
     FDLIMHTLTE HEIDTIVHFA AHSHVDNSFK NSLAFTETNV FGTHVLLECS RMYGKLKLFF
     HMSTDEVYGE IDTTDTSREV SLLCPTNPYA ATKAGAEHIV KSYFLSYKLP IIIARCNNVY
     GRNQYPEKLI PKFICSLLDG KKLHIQGTGN SRRNFIHAID VADAVDLVIN NGVIGETYNI
     GVTNEHSVLD VAQILCDIAG VNLENQLEYV PDRLFNDFRY NITNDKIKSL GWEQSRKDFK
     KELVELFDWY KVNRHRYNIP GSQ
 
 
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