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Database: UniProt
Entry: G8RIV7_MYCRN
LinkDB: G8RIV7_MYCRN
Original site: G8RIV7_MYCRN 
ID   G8RIV7_MYCRN            Unreviewed;       340 AA.
AC   G8RIV7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
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   OrderedLocusNames=MycrhN_0302 {ECO:0000313|EMBL:AEV70945.1};
OS   Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV70945.1, ECO:0000313|Proteomes:UP000005442};
RN   [1] {ECO:0000313|EMBL:AEV70945.1, ECO:0000313|Proteomes:UP000005442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB3 {ECO:0000313|EMBL:AEV70945.1,
RC   ECO:0000313|Proteomes:UP000005442};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA   Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL   Submitted (DEC-2011) 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; CP003169; AEV70945.1; -; Genomic_DNA.
DR   RefSeq; WP_014208765.1; NC_016604.1.
DR   AlphaFoldDB; G8RIV7; -.
DR   STRING; 710685.MycrhN_0302; -.
DR   KEGG; mrh:MycrhN_0302; -.
DR   PATRIC; fig|710685.3.peg.309; -.
DR   eggNOG; COG1089; Bacteria.
DR   HOGENOM; CLU_007383_14_0_11; -.
DR   OrthoDB; 9779041at2; -.
DR   Proteomes; UP000005442; 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};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00955};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005442}.
FT   DOMAIN          5..315
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   340 AA;  38169 MW;  86A6969EE009ECDC CRC64;
     MKRALIVGIT GQDGSYLAEL LLNKGYEVHG LIRRASTFNT SRIDHLYVDP HETGAQLFLH
     YGDLTDGTRL VTLLSTIEPD EVYNLAAQSH VRVSFDEPVH TGDTTGVGSI RLLEAVRLSR
     VQCRFYQASS SEMFGASPPP QSEQTVFYPR SPYGAAKVYS YWVTRNYREA YGLFAVNGIL
     FNHESPRRGE TFVTRKITRA VARIKAGVQE NLYMGNLDAV RDWGYAPEYV EGMWRMLQVA
     EPDDFVLATG RGFTVRDFVQ AAFDHAGLDW QRHVKFDERY LRPTEVDSLI GDASKAADAL
     GWKASVHTDE LARIMVDADI AAWECEGKPW IDKPTFSDGA
//
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