ID   CRYL1_PONAB             Reviewed;         319 AA.
AC   Q5RDZ2;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Lambda-crystallin homolog;
DE            EC=1.1.1.45 {ECO:0000250|UniProtKB:Q9Y2S2};
DE   AltName: Full=L-gulonate 3-dehydrogenase;
DE            Short=Gul3DH;
GN   Name=CRYL1;
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: Has high L-gulonate 3-dehydrogenase activity. It also
CC       exhibits low dehydrogenase activity toward L-3-hydroxybutyrate (HBA)
CC       and L-threonate. {ECO:0000250|UniProtKB:Q9Y2S2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-gulonate + NAD(+) = 3-dehydro-L-gulonate + H(+) + NADH;
CC         Xref=Rhea:RHEA:12889, ChEBI:CHEBI:13115, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57655, ChEBI:CHEBI:57945; EC=1.1.1.45;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y2S2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12890;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y2S2};
CC   -!- ACTIVITY REGULATION: Inhibited by malonate.
CC       {ECO:0000250|UniProtKB:Q9Y2S2}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y2S2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14755}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CR857749; CAH90015.1; -; mRNA.
DR   RefSeq; NP_001124956.1; NM_001131484.1.
DR   AlphaFoldDB; Q5RDZ2; -.
DR   SMR; Q5RDZ2; -.
DR   STRING; 9601.ENSPPYP00000005915; -.
DR   Ensembl; ENSPPYT00000006147; ENSPPYP00000005915; ENSPPYG00000005192.
DR   GeneID; 100171829; -.
DR   KEGG; pon:100171829; -.
DR   CTD; 51084; -.
DR   eggNOG; KOG2305; Eukaryota.
DR   GeneTree; ENSGT00390000007182; -.
DR   HOGENOM; CLU_009834_0_0_1; -.
DR   InParanoid; Q5RDZ2; -.
DR   OMA; RDNCLTH; -.
DR   OrthoDB; 840631at2759; -.
DR   TreeFam; TF313501; -.
DR   Proteomes; UP000001595; Chromosome 13.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0050104; F:L-gulonate 3-dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR022694; 3-OHacyl-CoA_DH.
DR   InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   PIRSF; PIRSF000105; HCDH; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P14755"
FT   CHAIN           2..319
FT                   /note="Lambda-crystallin homolog"
FT                   /id="PRO_0000232507"
FT   BINDING         16..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P14755"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q811X6"
FT   MOD_RES         111
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2S2"
SQ   SEQUENCE   319 AA;  35437 MW;  641CED57DA2BDE34 CRC64;
     MASSAAGCVV IVGSGVIGRS WAMLFASGGF QVKLYDIEQQ QIRNALENIR KEMKLLEQAG
     SLKGSLSVEE QLSLISGCPN IQEAVEGAMH IQECVPEDLE LKKKIFAQLD SIIDDRVILS
     SSTSCLMPSK LFAGLVHVKQ CIVAHPVNPP YYIPLVELVP HPETAPTTVD RTHALMKKIG
     QCPMRVQKEV AGFVLNRLQY AIISEAWRLV EEGIVSPSDL DLVMSEGLGM RYAFIGPLET
     MHLNAEGMLS YCDRYSEGMK HVLKTFGPIP EFSRATAEKV NQDMCMKVPD DPEHLAARRQ
     WRDECLMRLA KLKSQVQPQ