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Database: UniProt
Entry: A0A090LNM2_STRRB
LinkDB: A0A090LNM2_STRRB
Original site: A0A090LNM2_STRRB 
ID   A0A090LNM2_STRRB        Unreviewed;       610 AA.
AC   A0A090LNM2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=GDP-mannose 4,6-dehydratase {ECO:0000256|ARBA:ARBA00011989};
DE            EC=4.2.1.47 {ECO:0000256|ARBA:ARBA00011989};
DE   AltName: Full=GDP-D-mannose dehydratase {ECO:0000256|ARBA:ARBA00031085};
GN   ORFNames=SRAE_2000377700 {ECO:0000313|EMBL:CEF69125.1,
GN   ECO:0000313|WBParaSite:SRAE_2000377700.1,
GN   ECO:0000313|WormBase:SRAE_2000377700};
OS   Strongyloides ratti (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF69125.1};
RN   [1] {ECO:0000313|EMBL:CEF69125.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ED321 Heterogonic {ECO:0000313|EMBL:CEF69125.1};
RA   Aslett A.Martin.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000035682, ECO:0000313|WBParaSite:SRAE_2000377700.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC   ECO:0000313|WBParaSite:SRAE_2000377700.1};
RA   Martin A.A.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|WBParaSite:SRAE_2000377700.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (DEC-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000256|ARBA:ARBA00001937};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via
CC       de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00004912}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. GDP-mannose 4,6-dehydratase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009263}.
CC   -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B
CC       subfamily. {ECO:0000256|ARBA:ARBA00010694}.
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DR   EMBL; LN609529; CEF69125.1; -; Genomic_DNA.
DR   STRING; 34506.A0A090LNM2; -.
DR   EnsemblMetazoa; SRAE_2000377700.1; SRAE_2000377700.1; WBGene00264002.
DR   WBParaSite; SRAE_2000377700.1; SRAE_2000377700.1; WBGene00264002.
DR   WormBase; SRAE_2000377700; SRP11288; WBGene00264002; -.
DR   eggNOG; KOG1372; Eukaryota.
DR   OrthoDB; 5484740at2759; -.
DR   UniPathway; UPA00128; UER00190.
DR   Proteomes; UP000035682; Chromosome X.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019673; P:GDP-mannose metabolic process; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; 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   InterPro; IPR013657; SCL35B1-4/HUT1.
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   Pfam; PF08449; UAA; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        61..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        189..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        218..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          282..596
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   610 AA;  68898 MW;  125F2F90380F7409 CRC64;
     MDISSPVPLT ILTCTSCMFF IELLSKKKEN CMVFLTFCTF AFIAIHGLIF TSKFFTVKRN
     IPLRVYFKIA FIFFIVNLSN NQSLQYNISV PICIIFRSAS LLVNMAMGYL FLNKKYTLKK
     LISVVIVTLG IYSFIVVSDH SVPKKETTIS GFAIGITLLS VALILSSYLG ILQENMYKEY
     GKYPQEASFY TYLISLPYFL IFSNEICLAV VEFEVTNIIM IVLICLFQLF CINNVYILTT
     ELSSLGVTMV LTLRKFISVI ISVFYFGHNL SIMSEGSKKI ALITGITGQD GSYLAELLIA
     KGYSVHGIIR RSSTFNTHRI AHLYADPNIH KGSSTFQLHY GDMTDSSCLI KLISKIQPTE
     IYHLAAQSHV KVSFDLPEYT AEVDAVGTLR LLDAIVACNL QHKVKFYQAS TSELYGKVQE
     IPQKETTPFY PRSPYAVAKL YAFWIIKNYR EAYGIFACNG ILFNHESPRR GVQETLSLGN
     LDAKRDWGHA KEYVEAMWRI LQHDVADDFV ISTGKTESVR EFCNLAFAEI GMKLIWQGEG
     VNEVGIEEKT GKVRVRVDPN YYRPTEVDLL IGDPTKAKEV LGWEAKITLK ELVKEMVASD
     VELMKANPNA
//
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