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Lambda-crystallin (EC 1.1.1.45) (L-gulonate 3-dehydrogenase) (Gul3DH)

 CRYL1_RABIT             Reviewed;         319 AA.
P14755; A7VMV1;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 3.
23-MAY-2018, entry version 118.
RecName: Full=Lambda-crystallin;
EC=1.1.1.45;
AltName: Full=L-gulonate 3-dehydrogenase;
Short=Gul3DH;
Name=CRYL1; Synonyms=GUL3DH;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT ALA-2, AND PARTIAL PROTEIN
SEQUENCE.
TISSUE=Lens;
PubMed=3170592;
Mulders J.W.M., Hendriks W., Blankesteijn W.M., Bloemendal H.,
de Jong W.W.;
"Lambda-crystallin, a major rabbit lens protein, is related to
hydroxyacyl-coenzyme A dehydrogenases.";
J. Biol. Chem. 263:15462-15466(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
SUBUNIT, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS
OF ASP-36; SER-124; HIS-145; GLU-157 AND ASN-196, TISSUE SPECIFICITY,
AND SUBCELLULAR LOCATION.
TISSUE=Liver;
PubMed=15809331; DOI=10.1093/jb/mvi033;
Ishikura S., Usami N., Araki M., Hara A.;
"Structural and functional characterization of rabbit and human L-
gulonate 3-dehydrogenase.";
J. Biochem. 137:303-314(2005).
[3]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NAD.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of the rabbit L-gulonate 3-dehydrogenase.";
Submitted (NOV-2006) to the PDB data bank.
-!- FUNCTION: Functions as crystallin in the rabbit eye lens. Has high
L-gulonate 3-dehydrogenase activity.
{ECO:0000269|PubMed:15809331}.
-!- CATALYTIC ACTIVITY: L-gulonate + NAD(+) = 3-dehydro-L-gulonate +
NADH.
-!- ENZYME REGULATION: Inhibited by malonate and by inorganic
phosphate. {ECO:0000269|PubMed:15809331}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.011 mM for NAD {ECO:0000269|PubMed:15809331};
KM=0.0005 mM for NADH {ECO:0000269|PubMed:15809331};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15809331,
ECO:0000269|Ref.3}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15809331}.
-!- TISSUE SPECIFICITY: Detected in eye lens, kidney, liver, heart,
lung, brain and testis. {ECO:0000269|PubMed:15809331}.
-!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
{ECO:0000305}.
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EMBL; M22743; AAA31207.1; -; mRNA.
EMBL; AB359905; BAF76380.1; -; mRNA.
PIR; A31992; A31992.
RefSeq; NP_001075747.1; NM_001082278.1.
UniGene; Ocu.1849; -.
PDB; 3ADO; X-ray; 1.70 A; A=1-319.
PDB; 3ADP; X-ray; 1.85 A; A=1-319.
PDBsum; 3ADO; -.
PDBsum; 3ADP; -.
ProteinModelPortal; P14755; -.
SMR; P14755; -.
STRING; 9986.ENSOCUP00000011580; -.
MoonProt; P14755; -.
PRIDE; P14755; -.
GeneID; 100009108; -.
KEGG; ocu:100009108; -.
CTD; 51084; -.
eggNOG; KOG2305; Eukaryota.
eggNOG; COG1250; LUCA.
HOGENOM; HOG000141499; -.
HOVERGEN; HBG051126; -.
InParanoid; P14755; -.
KO; K13247; -.
BRENDA; 1.1.1.45; 1749.
SABIO-RK; P14755; -.
EvolutionaryTrace; P14755; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:InterPro.
GO; GO:0050104; F:L-gulonate 3-dehydrogenase activity; IDA:UniProtKB.
GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
Gene3D; 1.10.1040.10; -; 1.
InterPro; IPR022694; 3-OHacyl-CoA_DH.
InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
InterPro; IPR006108; 3HC_DH_C.
InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
InterPro; IPR013328; 6PGD_dom2.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF00725; 3HCDH; 1.
Pfam; PF02737; 3HCDH_N; 1.
PIRSF; PIRSF000105; HCDH; 1.
SUPFAM; SSF48179; SSF48179; 1.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00067; 3HCDH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Eye lens protein; NAD; Oxidoreductase;
Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed.
CHAIN 2 319 Lambda-crystallin.
/FTId=PRO_0000109322.
NP_BIND 16 17 NAD. {ECO:0000269|Ref.3}.
BINDING 36 36 NAD. {ECO:0000269|Ref.3}.
BINDING 97 97 NAD. {ECO:0000269|Ref.3}.
BINDING 102 102 NAD. {ECO:0000269|Ref.3}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000305|PubMed:3170592}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:Q811X6}.
MOD_RES 111 111 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2S2}.
MUTAGEN 36 36 D->R: Reduces enzyme activity and alters
specificity, so that NADP can be used as
cosubstrate.
{ECO:0000269|PubMed:15809331}.
MUTAGEN 124 124 S->A: Reduces enzyme activity 500-fold.
{ECO:0000269|PubMed:15809331}.
MUTAGEN 145 145 H->Q: Abolishes enzyme activity.
{ECO:0000269|PubMed:15809331}.
MUTAGEN 157 157 E->Q: No major effect on enzyme activity.
{ECO:0000269|PubMed:15809331}.
MUTAGEN 196 196 N->D,Q: Abolishes enzyme activity.
{ECO:0000269|PubMed:15809331}.
CONFLICT 252 252 C -> S (in Ref. 1; AAA31207).
{ECO:0000305}.
CONFLICT 288 288 V -> G (in Ref. 1; AAA31207).
{ECO:0000305}.
CONFLICT 308 308 R -> RE (in Ref. 1; AAA31207).
{ECO:0000305}.
STRAND 8 12 {ECO:0000244|PDB:3ADO}.
HELIX 16 27 {ECO:0000244|PDB:3ADO}.
STRAND 32 35 {ECO:0000244|PDB:3ADO}.
HELIX 39 58 {ECO:0000244|PDB:3ADO}.
STRAND 64 66 {ECO:0000244|PDB:3ADO}.
HELIX 68 73 {ECO:0000244|PDB:3ADO}.
STRAND 75 78 {ECO:0000244|PDB:3ADO}.
HELIX 81 84 {ECO:0000244|PDB:3ADO}.
TURN 85 87 {ECO:0000244|PDB:3ADO}.
STRAND 88 93 {ECO:0000244|PDB:3ADO}.
HELIX 99 110 {ECO:0000244|PDB:3ADO}.
STRAND 115 121 {ECO:0000244|PDB:3ADO}.
HELIX 128 132 {ECO:0000244|PDB:3ADO}.
HELIX 138 140 {ECO:0000244|PDB:3ADO}.
STRAND 141 146 {ECO:0000244|PDB:3ADO}.
TURN 150 152 {ECO:0000244|PDB:3ADO}.
STRAND 155 160 {ECO:0000244|PDB:3ADO}.
HELIX 166 178 {ECO:0000244|PDB:3ADO}.
STRAND 182 185 {ECO:0000244|PDB:3ADO}.
TURN 191 194 {ECO:0000244|PDB:3ADO}.
HELIX 195 211 {ECO:0000244|PDB:3ADO}.
HELIX 217 225 {ECO:0000244|PDB:3ADO}.
HELIX 228 232 {ECO:0000244|PDB:3ADO}.
HELIX 237 243 {ECO:0000244|PDB:3ADO}.
TURN 244 246 {ECO:0000244|PDB:3ADO}.
HELIX 248 264 {ECO:0000244|PDB:3ADO}.
HELIX 274 287 {ECO:0000244|PDB:3ADO}.
HELIX 292 315 {ECO:0000244|PDB:3ADO}.
SEQUENCE 319 AA; 35202 MW; C6F66B558BA422F6 CRC64;
MASPAAGDVL IVGSGLVGRS WAMLFASGGF RVKLYDIEPR QITGALENIR KEMKSLQQSG
SLKGSLSAEE QLSLISSCTN LAEAVEGVVH IQECVPENLD LKRKIFAQLD SIVDDRVVLS
SSSSCLLPSK LFTGLAHVKQ CIVAHPVNPP YYIPLVELVP HPETSPATVD RTHALMRKIG
QSPVRVLKEI DGFVLNRLQY AIISEAWRLV EEGIVSPSDL DLVMSDGLGM RYAFIGPLET
MHLNAEGMLS YCDRYSEGMK RVLKSFGSIP EFSGATVEKV NQAMCKKVPA DPEHLAARRE
WRDECLKRLA KLKRQMQPQ


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