ID B9EMX9_SALSA Unreviewed; 312 AA.
AC B9EMX9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Ketimine reductase mu-crystallin {ECO:0000256|ARBA:ARBA00015173};
DE EC=1.5.1.25 {ECO:0000256|ARBA:ARBA00012883};
DE AltName: Full=NADP-regulated thyroid-hormone-binding protein {ECO:0000256|ARBA:ARBA00033420};
GN Name=CRYM {ECO:0000313|EMBL:ACM08876.1};
GN Synonyms=crym {ECO:0000313|RefSeq:NP_001139957.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACM08876.1};
RN [1] {ECO:0000313|EMBL:ACM08876.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACM08876.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA Koop B.F.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACM08876.1, ECO:0000313|RefSeq:NP_001139957.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACM08876.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [3] {ECO:0000313|EMBL:ACM08876.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACM08876.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:NP_001139957.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-1,4-thiomorpholine-3-carboxylate + NAD(+) = 3,4-
CC dehydrothiomorpholine-3-carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:12504, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58517, ChEBI:CHEBI:176873;
CC EC=1.5.1.25; Evidence={ECO:0000256|ARBA:ARBA00029290};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-1,4-thiomorpholine-3-carboxylate + NADP(+) = 3,4-
CC dehydrothiomorpholine-3-carboxylate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:12500, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58517, ChEBI:CHEBI:176873;
CC EC=1.5.1.25; Evidence={ECO:0000256|ARBA:ARBA00029330};
CC -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC family. {ECO:0000256|ARBA:ARBA00008903}.
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DR EMBL; BT057004; ACM08876.1; -; mRNA.
DR RefSeq; NP_001139957.1; NM_001146485.1.
DR STRING; 8030.ENSSSAP00000063937; -.
DR PaxDb; 8030-ENSSSAP00000063937; -.
DR GeneID; 100286546; -.
DR KEGG; sasa:100286546; -.
DR CTD; 1428; -.
DR OrthoDB; 2501268at2759; -.
DR Proteomes; UP000087266; Chromosome ssa28.
DR GO; GO:0047127; F:thiomorpholine-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.1780.10; ornithine cyclodeaminase, domain 1; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003462; ODC_Mu_crystall.
DR InterPro; IPR023401; ODC_N.
DR PANTHER; PTHR13812; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR PANTHER; PTHR13812:SF19; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR Pfam; PF02423; OCD_Mu_crystall; 1.
DR PIRSF; PIRSF001439; CryM; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 2: Evidence at transcript level;
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
SQ SEQUENCE 312 AA; 34327 MW; BC6A183D2DAEFD70 CRC64;
MAEPPVLIRQ DEVEDLLHYK DLIPRLEIAL RKFSKLDSAE VIQPVRTTVP LQKYNGFLGL
MPAYLVHEDI LCTKLVCFYK RESGSTLPST QATVLLFDPE YGNVKAVMDG EVITAKRTAA
VSAISAKLLM PAKSDVLTIL GAGHQALSHY NVFTETFSFK EVRVWSRRKE TAERFAQSTQ
GHVTVLESVE EAVNGADVIV TVTGASEPVL FGQWVKPGAH VAAVGACRPD WRELDDVLMR
QAEVYVDSRE GAVAESGDII LSGAKVFAEL GEVLNGTRPA LREKTTVFKS LGMGIQDAVS
AKLVFEQWKN KH
//
