ID K9VT73_9CYAN Unreviewed; 313 AA.
AC K9VT73;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=GDP-L-fucose synthase {ECO:0000256|HAMAP-Rule:MF_00956};
DE EC=1.1.1.271 {ECO:0000256|HAMAP-Rule:MF_00956};
DE AltName: Full=GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase {ECO:0000256|HAMAP-Rule:MF_00956};
GN Name=fcl {ECO:0000256|HAMAP-Rule:MF_00956};
GN ORFNames=Cri9333_0121 {ECO:0000313|EMBL:AFZ11121.1};
OS Crinalium epipsammum PCC 9333.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC Crinalium.
OX NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ11121.1, ECO:0000313|Proteomes:UP000010472};
RN [1] {ECO:0000313|EMBL:AFZ11121.1, ECO:0000313|Proteomes:UP000010472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ11121.1,
RC ECO:0000313|Proteomes:UP000010472};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Crinalium epipsammum PCC 9333.";
RL Submitted (JUN-2012) 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|HAMAP-Rule:MF_00956}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose +
CC H(+) + NADPH; Xref=Rhea:RHEA:18885, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:57783, ChEBI:CHEBI:57964,
CC ChEBI:CHEBI:58349; EC=1.1.1.271; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00956};
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|HAMAP-Rule:MF_00956}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Fucose synthase subfamily. {ECO:0000256|ARBA:ARBA00005959,
CC ECO:0000256|HAMAP-Rule:MF_00956}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00956}.
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DR EMBL; CP003620; AFZ11121.1; -; Genomic_DNA.
DR RefSeq; WP_015201265.1; NC_019753.1.
DR AlphaFoldDB; K9VT73; -.
DR STRING; 1173022.Cri9333_0121; -.
DR KEGG; cep:Cri9333_0121; -.
DR PATRIC; fig|1173022.3.peg.131; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_18_0_3; -.
DR OrthoDB; 9811425at2; -.
DR UniPathway; UPA00128; UER00191.
DR Proteomes; UP000010472; Chromosome.
DR GO; GO:0050577; F:GDP-L-fucose synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0070401; F:NADP+ binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd05239; GDP_FS_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_00956; GDP_fucose_synth; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR028614; GDP_fucose/colitose_synth.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43238; GDP-L-FUCOSE SYNTHASE; 1.
DR PANTHER; PTHR43238:SF1; GDP-L-FUCOSE SYNTHASE; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00956};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00956};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00956};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00956}; Reference proteome {ECO:0000313|Proteomes:UP000010472}.
FT DOMAIN 11..242
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
FT ACT_SITE 141
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 15..21
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 145
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 168..171
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 184
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT SITE 112
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT SITE 114
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
SQ SEQUENCE 313 AA; 34857 MW; 9A2C631BAF32A63C CRC64;
MATVDLSNKR IVVTGGAGFL GRKVLAQLAS AGANPEKITV TRSHDCDLRI LENCQRAVDQ
QDIIIHLAAH VGGIGLNQAK PAELFYDNLM MGTQLIHAAY QAGVEKFVCV GTICAYPKFT
PVPFKEDDLW NGYPEETNAP YGVAKKALLV QLQSYRQQYG FNGIYLLPVN LYGPEDNFDP
KSSHVIPALI HKVHEAQQRG DKHLPVWGDG SPSREFLYVD DAALGVVVAT QDYDGAEPVN
LGTNYEITIR DLVELICELM GFQGEIIWEI DKPNGQPRRC LDTERAKQEF GFTAQVELKQ
GLKNTIDWYR HNQ
//
