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Database: UniProt
Entry: K9VVD2_9CYAN
LinkDB: K9VVD2_9CYAN
Original site: K9VVD2_9CYAN 
ID   K9VVD2_9CYAN            Unreviewed;       359 AA.
AC   K9VVD2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=GDP-mannose 4,6-dehydratase {ECO:0000256|ARBA:ARBA00011989, ECO:0000256|HAMAP-Rule:MF_00955};
DE            EC=4.2.1.47 {ECO:0000256|ARBA:ARBA00011989, ECO:0000256|HAMAP-Rule:MF_00955};
DE   AltName: Full=GDP-D-mannose dehydratase {ECO:0000256|HAMAP-Rule:MF_00955};
GN   Name=gmd {ECO:0000256|HAMAP-Rule:MF_00955};
GN   ORFNames=Cri9333_0120 {ECO:0000313|EMBL:AFZ11120.1};
OS   Crinalium epipsammum PCC 9333.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC   Crinalium.
OX   NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ11120.1, ECO:0000313|Proteomes:UP000010472};
RN   [1] {ECO:0000313|EMBL:AFZ11120.1, ECO:0000313|Proteomes:UP000010472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ11120.1,
RC   ECO:0000313|Proteomes:UP000010472};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Crinalium epipsammum PCC 9333.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-
CC       deoxy-D-mannose. {ECO:0000256|HAMAP-Rule:MF_00955}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00955};
CC   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000256|ARBA:ARBA00001937,
CC         ECO:0000256|HAMAP-Rule:MF_00955};
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. GDP-mannose 4,6-dehydratase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009263, ECO:0000256|HAMAP-Rule:MF_00955}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00955}.
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DR   EMBL; CP003620; AFZ11120.1; -; Genomic_DNA.
DR   RefSeq; WP_015201264.1; NC_019753.1.
DR   AlphaFoldDB; K9VVD2; -.
DR   STRING; 1173022.Cri9333_0120; -.
DR   KEGG; cep:Cri9333_0120; -.
DR   PATRIC; fig|1173022.3.peg.130; -.
DR   eggNOG; COG1089; Bacteria.
DR   HOGENOM; CLU_007383_14_0_3; -.
DR   OrthoDB; 9779041at2; -.
DR   Proteomes; UP000010472; Chromosome.
DR   GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070401; F:NADP+ binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019673; P:GDP-mannose metabolic process; IEA:InterPro.
DR   CDD; cd05260; GDP_MD_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
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   NCBIfam; TIGR01472; gmd; 1.
DR   PANTHER; PTHR43715:SF1; GDP-MANNOSE 4,6 DEHYDRATASE; 1.
DR   PANTHER; PTHR43715; GDP-MANNOSE 4,6-DEHYDRATASE; 1.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00955, ECO:0000313|EMBL:AFZ11120.1};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00955};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010472}.
FT   DOMAIN          8..323
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   359 AA;  40849 MW;  2F3B3BF68AB55779 CRC64;
     MSERKIALIT GITGQDGSYL SELLLDKGYE VHGIIRRTST FNTDRIDHIY VDPHNEQARL
     FLHYGDLTDG TTLRRILEEV KPVEIYNLGA QSHVKVSFDS PEYTVDSVGM GTLRLLEAIR
     DYQHRTGIQV RFYQAGSSEM FGKVQEVPQK ETTPFYPRSP YACAKVYAHW QTVNYRESYG
     LFACNGILFN HESPRRGETF VTRKITRAIA RIIAGKQKNT FLGNLDAKRD WGYAKDYVKA
     MWLMLQQDQP DDYVVATGET HSVGEFLNLA FGYVNLDWHK YVEFDGRYLR PAEVDLLIGD
     ATKTKQKLGW QPSVTFPELV ALMVEADLQA LGLTSPNNNS SNSFPDIATI RQNVGEMHD
//
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