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Database: UniProt
Entry: A0A3R9MJ73_9RHOB
LinkDB: A0A3R9MJ73_9RHOB
Original site: A0A3R9MJ73_9RHOB 
ID   A0A3R9MJ73_9RHOB        Unreviewed;       373 AA.
AC   A0A3R9MJ73;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
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   ECO:0000313|EMBL:RSK32916.1};
GN   ORFNames=EJA01_11385 {ECO:0000313|EMBL:RSK32916.1};
OS   Rhodovulum robiginosum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodovulum.
OX   NCBI_TaxID=68292 {ECO:0000313|EMBL:RSK32916.1, ECO:0000313|Proteomes:UP000275159};
RN   [1] {ECO:0000313|EMBL:RSK32916.1, ECO:0000313|Proteomes:UP000275159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12329 {ECO:0000313|EMBL:RSK32916.1,
RC   ECO:0000313|Proteomes:UP000275159};
RA   Gupta D., Guzman M.S., Bose A.;
RT   "Draft genome sequence of a marine photoferrotrophic bacterium, Rhodovulum
RT   robiginosum.";
RL   Submitted (DEC-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RSK32916.1}.
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DR   EMBL; RWGU01000048; RSK32916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R9MJ73; -.
DR   OrthoDB; 9779041at2; -.
DR   Proteomes; UP000275159; Unassembled WGS sequence.
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:RSK32916.1};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00955};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275159}.
FT   DOMAIN          6..346
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   373 AA;  41972 MW;  BE836BFA86329BBB CRC64;
     MAKRALITGI TGQDGSYLAE LLLEKGYEVH GIKRRASLFN TQRIDHVFQD PHEPNPKLKL
     HYGDLSDTSN LTRILCEVEP DEVYNLGAQS HVAVSFEAPE YTADVDAIGT LRLLEAIRFL
     GFEKKTRFYQ ASTSELYGLV QEIPQTETTP FHPRSPYAVA KLYAYWITVN YREAYGMYAC
     NGILFNHESP RRGETFVTRK ITRGLANIAQ GLEDCLYMGN IDALRDWGHA KDYVRMQWMM
     LQQDVPEDFV IATGVQYSVR EFIVWSAAEL GLTLEFSGEG VDEIATVAAN EGDKAPSVKV
     GDVIMRIDPR YFRPAEVETL LGDPSKAKAK LGWTPVITVQ EMCAEMVRED LKVAQRHAHL
     KSHGFDMPIA QSG
//
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