ID L5JTD2_PTEAL Unreviewed; 314 AA.
AC L5JTD2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ORFNames=PAL_GLEAN10000993 {ECO:0000313|EMBL:ELK02257.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK02257.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB031144; ELK02257.1; -; Genomic_DNA.
DR RefSeq; XP_006924222.1; XM_006924160.2.
DR AlphaFoldDB; L5JTD2; -.
DR STRING; 9402.L5JTD2; -.
DR GeneID; 102893293; -.
DR KEGG; pale:102893293; -.
DR CTD; 1428; -.
DR eggNOG; KOG3007; Eukaryota.
DR InParanoid; L5JTD2; -.
DR OrthoDB; 2501268at2759; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000010552}.
SQ SEQUENCE 314 AA; 33777 MW; 7E918B5A6174FBE8 CRC64;
MSWAPAFLSA AEVQNHLRSS SLLIPPLEAA LANFSSGLDG GVTQPVRTVV PVAKHNGFLG
VMPVYSAAED ALTTKLVTFY EGHSTTSSVP SHQATVLLFE PSNGSLLAVM DGNVITAKRT
AAVSAIATKF LKPPSSEVLC ILGAGVQAYS HYEIFTEQFS FKEVRIWNRT RENAEKFADT
VQGEVRVCSS VQEAVTDADV IITVTMATEP ILFGEWVKLG AHINAIGASR PDWRELDDKL
MKQAVLYVDS REAALKESGD VLLSGAEIFA ELGEVVKGVK PAYCEKTTVF KSLGMAVEDM
VAAKLVYDSW SSGK
//
