ENOF1_PONAB
ID ENOF1_PONAB Reviewed; 443 AA.
AC Q5RAT4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Mitochondrial enolase superfamily member 1;
DE EC=4.2.1.68 {ECO:0000250|UniProtKB:Q7L5Y1};
DE AltName: Full=L-fuconate dehydratase;
GN Name=ENOSF1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-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 -!- PTM: Could be sumoylated. {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; CR858928; CAH91126.1; -; mRNA.
DR RefSeq; NP_001125659.1; NM_001132187.1.
DR AlphaFoldDB; Q5RAT4; -.
DR SMR; Q5RAT4; -.
DR STRING; 9601.ENSPPYP00000010153; -.
DR GeneID; 100172579; -.
DR KEGG; pon:100172579; -.
DR CTD; 55556; -.
DR eggNOG; ENOG502QU7C; Eukaryota.
DR InParanoid; Q5RAT4; -.
DR OrthoDB; 933480at2759; -.
DR Proteomes; UP000001595; Unplaced.
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:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
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; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
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.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 2: Evidence at transcript level;
KW Isomerase; Lyase; Magnesium; Metal-binding; Mitochondrion; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..443
FT /note="Mitochondrial enolase superfamily member 1"
FT /id="PRO_0000331653"
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"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L5Y1"
SQ SEQUENCE 443 AA; 49792 MW; 2FD66C8F41124C54 CRC64;
MVRGRIFRLS VRDVRFPTSL GGHGSDAMHT DPDYSAAYVV IETDAEDGIK GCGITFTLGK
GTEVVVCAVN ALAHHVLNKD LKDIVGDFRG FYRQLTSDGQ PRWIGPEKGV VHLATAAVLN
AVWDLWAKQE GKPVWKLLVD MDPRTLVSCI DFRYITDVLT EEDALEILQK GQVGKKEREK
QMLAQGYPAY TTSCAWLGYS DDTLKQLCAQ ALKDGWTRFK VKVGADLQDD VRRCQIIRDM
IGLEKTLMMD ANQRWDVPEA VEWMSKLAKF KPLWIEEPTS PDDILGHATI SKALVPLGIG
IATGEQCHNR VIFKQLLQAK ALQFLQIDSC RLGSVNENLS VLLMAKKFEI PVCPHAGGVG
LCELVQHLII FDYISVSASL ENRMCEYVDH LHEHFKYPVM IQRASYMPPK DPGYSTEMKE
ESVKKHQYPD GEVWKKLLAA QEN
