ID A0A0V1PIV6_9BILA Unreviewed; 1181 AA.
AC A0A0V1PIV6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:KRZ96153.1};
GN ORFNames=T08_5371 {ECO:0000313|EMBL:KRZ96153.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ96153.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ96153.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ96153.1};
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:KRZ96153.1}.
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DR EMBL; JYDM01000009; KRZ96153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1PIV6; -.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00128; UER00191.
DR Proteomes; UP000054924; 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:UP000054924};
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 493..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 589..611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 631..649
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..233
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
FT DOMAIN 664..744
FT /note="Alpha-N-acetylglucosaminidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12971"
FT DOMAIN 810..966
FT /note="Alpha-N-acetylglucosaminidase tim-barrel"
FT /evidence="ECO:0000259|Pfam:PF05089"
FT DOMAIN 976..1175
FT /note="Alpha-N-acetylglucosaminidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12972"
SQ SEQUENCE 1181 AA; 134721 MW; 7124EA50AD3AB487 CRC64;
MVDTVLVTGA SGLIGRAMQA VIAEAAKNFE VNMNWIFVSS KDADLTDYVQ TKRMFQVNKP
TAVIHLAAKV GGLFCNLDNN LSFFRQNMMI NDNVLRCAHE HNVKRVISCL STCIFPDNTT
YPLDENMIHL GPPHESNMGY AYAKRMLDML SSLYNRQYGY CYTSIIPCNV FGPHDNFSLK
NGHSIPALIH KCYLAKENNT PLVVFGTGKP LRQYIYSLDL ARLIIWALEN YKDPTPIIFA
TDEADEVTIE HVAKSIAQGM QFQGPILFDT SKSDGQFKKT SSNAKMRSYL PDFKFTPFDK
AIQETAQWFT ANFNSARNTD LCKVFMMCCN FRIHVAQFLL YSLIVISTHL FFYGIRYNME
SFLLGICTYQ PENQIELVWF GNVTFGRIDF FELNVLLSII GDIPELFIIE LQGDLELSNS
KSLSGTLISA FSCNKQGNAF MIVGRHILRG KVEQLQRPIA LVKQCSADVS TSTHQDCLQH
GIREIMSFRD GYLFLYNTVQ FIGWSLIFWK IVIGLLTGIT LNHVYSVVGC QVEFFQTLAL
LEIVHSYTGL VRSPTVTTAI QVLSRLFILW PITHCVVEAQ SSLGTYTLFI GLYPLGVAGE
LVAVFAAMGP IGRRKLFTLE MPNMFNMSFN FYYSLFFIIP LYIPLLGSVD DLKPSASAFE
QISAVQKLLN RISFGLADFY VLEIDHTLSD NSEMVLVKSW KDVRNRTLIK GTSGVALAFG
VNAHLRNMYD VHIAWDGIRV ELPAIVSPPH KQMMFKSIGR YRYFGNVCTF SYSFAWWNWS
RWEYFIDWMA LNGINLPLAH VGNEVVWKSL ENYFGLFHAY SADPFNEMVP NTFDVMFLRN
VSFAIYNVMV LQSWMFLSSE RWLENENAKH FLTAVPTGSI LVVDLYAEEY PLYEKFSGFY
NQPFIWCMLH NFGGVQGLYG NLARINQKLA DVSTVSNISM VGTGLSMEGI DQNYVVYQMA
LDRFWSPNNQ KGVGITKSIY TAWGAFLQSS RTCQESEIYI NDLVELTKHA LMLTGAKLYE
QLQASYIRKY GQEFLENAAA VERVLSDLEW ISKTHSRSML SKWIEIARSN GKTAAQSDQL
EENLRMQVTI WGPQGEIVDY ARKQWAALFS EYYLPRWRLF FAHLYADILQ LETFNQTLLN
SRLFHEIELP FALQKIPNID QPTGNTVVVS KILYNRYGII K
//
