ID R0A9Z9_9FIRM Unreviewed; 356 AA.
AC R0A9Z9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=HMPREF1085_03441 {ECO:0000313|EMBL:ENZ48891.1};
OS Enterocloster bolteae 90A9.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Enterocloster.
OX NCBI_TaxID=997894 {ECO:0000313|EMBL:ENZ48891.1, ECO:0000313|Proteomes:UP000013126};
RN [1] {ECO:0000313|EMBL:ENZ48891.1, ECO:0000313|Proteomes:UP000013126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90A9 {ECO:0000313|EMBL:ENZ48891.1,
RC ECO:0000313|Proteomes:UP000013126};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Courvalin P., Lambert T.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Clostridium bolteae 90A9.";
RL Submitted (JAN-2013) 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:ENZ48891.1}.
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DR EMBL; AGYH01000011; ENZ48891.1; -; Genomic_DNA.
DR RefSeq; WP_002576472.1; NZ_KB851182.1.
DR AlphaFoldDB; R0A9Z9; -.
DR PATRIC; fig|997894.4.peg.3613; -.
DR HOGENOM; CLU_007383_14_0_9; -.
DR OrthoDB; 9779041at2; -.
DR Proteomes; UP000013126; 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};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00955}.
FT DOMAIN 6..334
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
FT BINDING 125
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00955"
SQ SEQUENCE 356 AA; 40256 MW; 0EDB4B1C9F6465CE CRC64;
MSKIALITGI TGQDGSYLAE FLLNKGYEVH GLVRRHSISN TERIDHIINS EYNRVKFFLH
YADVTDSSNL MRLIAEIRPT EVYNLAAQSH VGISFEVPEY TAEATGVSTL KLLEALRVNG
GNCRYYQAST SELFGGLENT APQSEATPFY PKSPYGAAKL YAYWITVNYR ESYNMFACNG
ILFNHESPRR GENFVTRKIT MALANIIAGK QNKLSLGNMD AKRDWGFAGD YVEGMWRILQ
HDVPGDFVLA TNETHTVRQF VEAACEELGI EIRWEGVGVE EKGYDAMTGR LLVDVNPEFY
RPAEVEFLWG DPSKAEKELN WKRKVDFKGL VSMMMNADLK AVAGMSCKEY RDRKLD
//
