ENOF1_BOVIN
ID ENOF1_BOVIN Reviewed; 443 AA.
AC Q2KIA9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) 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; BC112706; AAI12707.1; -; mRNA.
DR RefSeq; NP_001040015.1; NM_001046550.2.
DR AlphaFoldDB; Q2KIA9; -.
DR SMR; Q2KIA9; -.
DR STRING; 9913.ENSBTAP00000031013; -.
DR PaxDb; Q2KIA9; -.
DR PRIDE; Q2KIA9; -.
DR Ensembl; ENSBTAT00000076666; ENSBTAP00000056727; ENSBTAG00000007000.
DR GeneID; 615106; -.
DR KEGG; bta:615106; -.
DR CTD; 55556; -.
DR VEuPathDB; HostDB:ENSBTAG00000007000; -.
DR VGNC; VGNC:28501; ENOSF1.
DR eggNOG; ENOG502QU7C; Eukaryota.
DR GeneTree; ENSGT00390000014290; -.
DR HOGENOM; CLU_030273_2_0_1; -.
DR InParanoid; Q2KIA9; -.
DR OMA; SGAIDVC; -.
DR OrthoDB; 933480at2759; -.
DR TreeFam; TF300529; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000007000; Expressed in cortex of kidney and 106 other tissues.
DR ExpressionAtlas; Q2KIA9; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
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:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
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_0000331651"
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; 49621 MW; C3D921D57C410AE2 CRC64;
MVHGRVSRLS VHDVRFPTSL GGHGSDAMHT DPDYSAAYVV LETDAEDGLK GYGITFTLGR
GTEVVVCAVN ALAPHVLNKD LGEIVGDFRG FYRQLTSDGQ LRWIGPEKGV VHLATAAVLN
AVWDLWAKQE GKPLWKLLVD MDPRTLVSCI DFRYITDVLT EEEACEILRQ SQVGKKEREE
QMLAHGYPAY TTSCAWLGYP DATLKQLCSE ALKDGWTRFK VKVGADLQDD IRRCRLVRNM
IGPEKTLMMD ANQRWDVPEA VEWMTKLAEF KPLWIEEPTS PDDILGHAAI SKALAPLGIG
VATGEQCHNR VIFKQLLQAK ALKFLQIDSC RLGSVNENLS VLLMAKKFEI PVCPHAGGVG
LCELVQHLII FDFISVSASL QDRMCEYVDH LHEHFKYPVL IREAAYMPPK DAGYSTEMKE
DSVKRHRYPD GEVWKKLLSA QGN
