ID   GMD1_CAEBR              Reviewed;         377 AA.
AC   A8Y0L5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=GDP-mannose 4,6 dehydratase 1;
DE            EC=4.2.1.47;
DE   AltName: Full=Bacillus thuringiensis toxin-resistant protein 1;
DE            Short=Bt toxin-resistant protein 1;
DE   AltName: Full=GDP-D-mannose dehydratase;
DE            Short=GMD;
GN   ORFNames=CBG21737 {ECO:0000312|WormBase:CBG21737a};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-
CC       deoxy-D-mannose. Involved in susceptibility to pore-forming crystal
CC       toxins in conjunction with bre-2, bre-3 and bre-4. Has a role in
CC       determining brood size (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O;
CC         Xref=Rhea:RHEA:23820, ChEBI:CHEBI:15377, ChEBI:CHEBI:57527,
CC         ChEBI:CHEBI:57964; EC=4.2.1.47;
CC   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P93031};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via
CC       de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 1/2.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. GDP-mannose 4,6-dehydratase subfamily. {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; HE600966; CAP38434.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8Y0L5; -.
DR   SMR; A8Y0L5; -.
DR   STRING; 6238.CBG21737; -.
DR   WormBase; CBG21737a; CBP11948; WBGene00040436; -.
DR   eggNOG; KOG1372; Eukaryota.
DR   HOGENOM; CLU_007383_14_0_1; -.
DR   InParanoid; A8Y0L5; -.
DR   OMA; TDCLYLG; -.
DR   OrthoDB; 877551at2759; -.
DR   UniPathway; UPA00128; UER00190.
DR   Proteomes; UP000008549; Chromosome IV.
DR   GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IBA:GO_Central.
DR   GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019673; P:GDP-mannose metabolic process; IBA:GO_Central.
DR   HAMAP; MF_00955; GDP_Man_dehydratase; 1.
DR   InterPro; IPR006368; GDP_Man_deHydtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43715; PTHR43715; 1.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01472; gmd; 1.
PE   3: Inferred from homology;
KW   Insecticide resistance; Lyase; NADP; Reference proteome.
FT   CHAIN           1..377
FT                   /note="GDP-mannose 4,6 dehydratase 1"
FT                   /id="PRO_0000324672"
FT   ACT_SITE        161
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        163
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        185
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         35..40
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         92..93
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         114..118
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   377 AA;  42216 MW;  998825857EBA2804 CRC64;
     MEGLEACIGQ SHEVMTTPAA ELAAFRARKV ALITGISGQD GSYLAELLLS KGYKVHGIIR
     RSSSFNTARI EHLYSNPMTH NGDSSFSLHY GDMTDSSCLI KLISTIEPTE VYHLAAQSHV
     KVSFDLPEYT AEVDAVGTLR LLDAIHACRL TEKVRFYQAS TSELYGKVQE IPQSEKTPFY
     PRSPYAVAKM YGYWIVVNYR EAYKMFACNG ILFNHESPRR GETFVTRKIT RSVAKISLGQ
     QESIELGNLS ALRDWGHARE YVEAMWRILQ HDAPDDFVIA TGKQFSVREF CNLAFAEIGE
     VLEWEGEGVE EVGKNKDGIV RVKVSPKYYR PTEVETLLGN PEKAKKTLGW EAKVTVPELV
     KEMVASDIAL MKANPMA