ID A0A087R6I6_APTFO Unreviewed; 256 AA.
AC A0A087R6I6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 21.
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};
DE Flags: Fragment;
GN ORFNames=AS27_15037 {ECO:0000313|EMBL:KFM09090.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM09090.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM09090.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM09090.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL226142; KFM09090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087R6I6; -.
DR STRING; 9233.A0A087R6I6; -.
DR Proteomes; UP000053286; 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 SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053286}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM09090.1"
FT NON_TER 256
FT /evidence="ECO:0000313|EMBL:KFM09090.1"
SQ SEQUENCE 256 AA; 27408 MW; 722E9AAE8EFFCADC CRC64;
FLGVMPAYSA ADDALTTKLV TFYEHKKDSS VPSHQATVLL LDPRNGSLKA VLDGSVITAK
RTAAVSAIAT KMLMPAFAEV LCILGAGVQA YSHYDIFTEL FTFKEVRIWN RTKEKAVKFA
NSVNGPVQVC SSAQEAVSGA DVIITVTMAT TPILFGDWVK PGAHINAVGA SRPDWRELDD
EVMKNSVLFV DSREAALTES GDVILSGAEI FAELGEVVKG TKPALPEKTT VFKSLGMAVE
DTVAAKFVYD SWSAGN
//
