ENOF1_XENLA
ID ENOF1_XENLA Reviewed; 445 AA.
AC Q6INX4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Mitochondrial enolase superfamily member 1;
DE AltName: Full=L-fuconate dehydratase;
DE EC=4.2.1.68 {ECO:0000250|UniProtKB:Q7L5Y1};
GN Name=enosf1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the catabolism of L-fucose, a sugar that is
CC part of the carbohydrates that are attached to cellular glycoproteins.
CC Catalyzes the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by
CC the abstraction of the 2-proton to generate an enediolate intermediate
CC that is stabilized by the magnesium ion. May down-regulate thymidylate
CC synthase activity, possibly already at the RNA level, by promoting the
CC degradation of TYMS mRNA via an antisense RNA-based mechanism.
CC {ECO:0000250|UniProtKB:Q7L5Y1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-fuconate = 2-dehydro-3-deoxy-L-fuconate + H2O;
CC Xref=Rhea:RHEA:22772, ChEBI:CHEBI:15377, ChEBI:CHEBI:21291,
CC ChEBI:CHEBI:37448; EC=4.2.1.68;
CC Evidence={ECO:0000250|UniProtKB:Q7L5Y1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q7L5Y1};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q7L5Y1};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q7L5Y1}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. ENOSF1 subfamily. {ECO:0000305}.
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DR EMBL; BC072148; AAH72148.1; -; mRNA.
DR RefSeq; NP_001085066.1; NM_001091597.1.
DR AlphaFoldDB; Q6INX4; -.
DR SMR; Q6INX4; -.
DR DNASU; 432136; -.
DR GeneID; 432136; -.
DR KEGG; xla:432136; -.
DR CTD; 432136; -.
DR Xenbase; XB-GENE-940743; enosf1.S.
DR OrthoDB; 933480at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 432136; Expressed in kidney and 19 other tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0050023; F:L-fuconate dehydratase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0044275; P:cellular carbohydrate catabolic process; ISS:UniProtKB.
DR CDD; cd03324; rTSbeta_L-fuconate_dehydratase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR034610; L-fuconate_dehydratase.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDF00111; L-fuconate_dehydratase; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
PE 2: Evidence at transcript level;
KW Isomerase; Lyase; Magnesium; Metal-binding; Mitochondrion;
KW Reference proteome.
FT CHAIN 1..445
FT /note="Mitochondrial enolase superfamily member 1"
FT /id="PRO_0000331654"
FT ACT_SITE 222
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT ACT_SITE 355
FT /evidence="ECO:0000255"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q7L5Y1"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q7L5Y1"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q7L5Y1"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT BINDING 355..357
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
SQ SEQUENCE 445 AA; 50247 MW; 3C1682085F6C298A CRC64;
MITGKITCLH ITDVRFPTSL DQHGSDAMHT DPDYSAAYVV IETDAADGLK GHGLTFTLGK
GTEVVVCAVR ALSRHVIGKA LEDIVNNFRD FYRQLTSDGQ LRWIGPEKGA VQLATAAVLN
AVWDLWAKKE KKPLWKLLVD MDPHQLVSCI DFRYITDALT EEEALKILQN GKQGQRDREE
HMLTSGYPAY TTSCAWLGYS DEQLKKLCSD ALKEGWTRFK VKVGADLKDD IRRCELIRDM
IGPDNIMMLD ANQRWDVQEA ISWVKDLAKY KPLWIEEPTS PDDILGHATI SKELSPVNIG
VATGEQCHNR VMFKQFLQAK ALQYLQIDSC RLGSVNENLS VLLMAKKFNV PVCPHAGGVG
LCELVQHLIL FDYICVSGSL DNRMCEYVDH LHEHFTYPVI INRAAYMPPK DPGYSTEMKE
ESVLQYQFPD GAVWKKLILE KKVEV
