ID A0A0V1A7B3_9BILA Unreviewed; 1392 AA.
AC A0A0V1A7B3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase {ECO:0000256|ARBA:ARBA00032995};
DE EC=1.1.1.271 {ECO:0000256|ARBA:ARBA00012371};
DE EC=4.2.1.134 {ECO:0000256|ARBA:ARBA00013122};
GN Name=TSTA3 {ECO:0000313|EMBL:KRY20661.1};
GN ORFNames=T12_15296 {ECO:0000313|EMBL:KRY20661.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY20661.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY20661.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY20661.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the two-step NADP-dependent conversion of GDP-4-
CC dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a
CC reductase reaction. {ECO:0000256|ARBA:ARBA00002870}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via
CC de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004883}.
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. Fucose synthase subfamily. {ECO:0000256|ARBA:ARBA00005959}.
CC -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase HACD
CC family. {ECO:0000256|ARBA:ARBA00007811}.
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:KRY20661.1}.
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DR EMBL; JYDQ01000023; KRY20661.1; -; Genomic_DNA.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00128; UER00191.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050577; F:GDP-L-fucose synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0102158; F:very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05239; GDP_FS_SDR_e; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 1.20.120.670; N-acetyl-b-d-glucoasminidase; 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_00956; GDP_fucose_synth; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR028614; GDP_fucose/colitose_synth.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR007781; NAGLU.
DR InterPro; IPR024732; NAGLU_C.
DR InterPro; IPR024240; NAGLU_N.
DR InterPro; IPR024733; NAGLU_tim-barrel.
DR InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR PANTHER; PTHR12872; ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR PANTHER; PTHR12872:SF1; ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR Pfam; PF01370; Epimerase; 1.
DR Pfam; PF05089; NAGLU; 1.
DR Pfam; PF12972; NAGLU_C; 1.
DR Pfam; PF12971; NAGLU_N; 1.
DR Pfam; PF04387; PTPLA; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 486..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 565..587
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..234
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
FT DOMAIN 648..728
FT /note="Alpha-N-acetylglucosaminidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12971"
FT DOMAIN 792..1038
FT /note="Alpha-N-acetylglucosaminidase tim-barrel"
FT /evidence="ECO:0000259|Pfam:PF05089"
FT DOMAIN 1059..1337
FT /note="Alpha-N-acetylglucosaminidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12972"
SQ SEQUENCE 1392 AA; 159139 MW; C3351131B4925755 CRC64;
MVDTVLVTGA SGLIGRAMQA VIAEAAKNYE VNMNWIFVSS KDADLTDYVQ TKRMFRVNKP
TAVIHLAAKV GGLFCNLDNN LSFFRENMMI NDNVLRCAHE HNVKRVISCL STCIFPDNTT
YPLDENMIHL GPPHESNMGY AYAKRMLDML SSLYNRQYGY CYTSIIPCNV FGPHDNFSLK
NGHSIPALIH KCYLAKENNT PLVVFGTGKP LRQYIYSLDL ARLIIWALEN YKEPTPIIFA
TDEADEVTIE HVAKSIAQGM QFQGPILFDT SKSDGQFKKT SSNAKMRSYL PDFKFTPFDK
AIQETAEWFT ANFASARNTD LCKVFMMCCN FRIHVAQFLL YSLIVISTHL FFYGIRYDME
SFLLGICTSQ PENQIELVWF GLIGQLDCFE SFYYYSTEIG DIPELFIIEL QGDLELSNSK
SLSGTLISAF SCNKQGNAFM IIGRHILRGK VEQLQRPIAL VKQCSADVST STHQDCLQHG
IRWSLIFWKI VIGLLTGITL NHVYSVVGCQ VEFFQTLALL EIVHSYTGLV RSPTVTTAIQ
VLSRLFILWP ITHCVVEAQS SLGTYTLFIG LYPLGVAGEL LAVFAAMGPI GRRKLFTLEM
PNIFNMSFNF YYSLVSHVIH VHAEATKEIL GSVDHLKPSA SALEQISAVQ KLLNRISFGL
ADFYVLEIDR TLSDNSEMVL VKSWKDIRNQ TLIKGTSGVA LAFGVNAHLR NMYDVHIAWD
GIRVELPAIV SPPHKQMMFK SIGRYRYFGN VCTFSYSFAW WNWSRWEYFI DWMALNGINL
PLAHVGNEVV WKSWQGPLTE TWHQDQLVLQ KRILKRMVEF GMLPILPAFA GHVPDGFRRI
FPTANLLSAK CWIFNSTYSC LKFVHPSDPL FLQIGKAYMQ KLENYFGLFH AYSADPFNEM
VPNTFDVMFL RNVSFAIYNV MVLQSWMFLS SERWLENENA KHFLTAVPTG SILVVDLYAE
EYPLYEKFSG FYNQPFIWCM LHNFGGVQGL YGNLARINQK LADVSTVSNI SMVGTGLSME
GIDQNYVVYQ MALDRFWSPN NRKVDLAAWY PYIFGMIVQY CIQRYGRLET NVISACKLLL
NNVYCAEHIF FHCKLNSVID EDTRNWLKNR ILSNDHHNIG ILTLRPKFGM KEQGVGITKS
IYTAWGAFLQ SSRTCQESEI YINDLVELTK HALMLTGAKL YEQLQASYIR KYGQEFLENA
AAVEQVLSDL EWISKTHSRS MLSKWIEIAR ANGKTVAQSD QLEENLRMQV TIWGPQGEIV
DYARKQWAAL FSEYYLPRWR LFFAHLYADI LQLETFNQTL LNSRLFHEIE LPFALQKIPN
IDQPTGNTVV VSKILYNHMN NEEKSENADG TKQNNKREKL VTSNSKKFQC TKTGFERCAM
QITIAIKVPY RQ
//
