ID A0A0A7PM36_9SPHN Unreviewed; 365 AA.
AC A0A0A7PM36;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=noeL {ECO:0000313|EMBL:AJA09002.1};
GN Synonyms=gmd {ECO:0000256|HAMAP-Rule:MF_00955};
GN ORFNames=SKP52_10485 {ECO:0000313|EMBL:AJA09002.1};
OS Sphingopyxis fribergensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1515612 {ECO:0000313|EMBL:AJA09002.1, ECO:0000313|Proteomes:UP000030907};
RN [1] {ECO:0000313|EMBL:AJA09002.1, ECO:0000313|Proteomes:UP000030907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kp5.2 {ECO:0000313|EMBL:AJA09002.1,
RC ECO:0000313|Proteomes:UP000030907};
RX PubMed=26040579; DOI=10.1099/ijs.0.000371;
RA Oelschlagel M., Ruckert C., Kalinowski J., Schmidt G., Schlomann M.,
RA Tischler D.;
RT "Description of Sphingopyxis fribergensis sp. nov. - a soil bacterium with
RT the ability to degrade styrene and phenylacetic acid.";
RL Int. J. Syst. Evol. Microbiol. 65:3008-3015(2015).
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 ---------------------------------------------------------------------------
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; CP009122; AJA09002.1; -; Genomic_DNA.
DR RefSeq; WP_039574573.1; NZ_CP009122.1.
DR AlphaFoldDB; A0A0A7PM36; -.
DR STRING; 1515612.SKP52_10485; -.
DR KEGG; sphk:SKP52_10485; -.
DR HOGENOM; CLU_007383_14_0_5; -.
DR OrthoDB; 9779041at2; -.
DR Proteomes; UP000030907; 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:AJA09002.1};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00955}.
FT DOMAIN 6..336
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 365 AA; 41203 MW; D07CF5F8057BFE96 CRC64;
MTKTALITGV TGQDGAYLAE LLLAKGYQVH GVKRRSSSFN TGRIDHIYQD PHESAAKLHL
HYGDMTDSTN LIRIVQEVAP DEIYNLAAQS HVQVSFDTPE YTANADAIGT LRLLEAIKIL
GLTQKTRFYQ ASTSELYGLV QEVPQRETTP FYPRSPYAAA KLYAYWITVN YREAYDMFAS
NGILFNHESP IRGETFVTRK ITRAVSAIHL GIQEKLWLGN LDAKRDWGHA RDYVEGMWRI
LQHERADDFV LATGQTQTVR HFVERAFAHV DITLDWQGTG VDERGVCAKT GKVLVEVDPR
YFRPTEVELL IGDPAKAKAE LGWVAETSFE QLVTDMMDAD LKTVAREAEH RRVDEEQSLQ
PRSAA
//
