ID S9YRE3_CAMFR Unreviewed; 329 AA.
AC S9YRE3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=CB1_000307031 {ECO:0000313|EMBL:EPY86525.1};
OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY86525.1, ECO:0000313|Proteomes:UP000030684};
RN [1] {ECO:0000313|EMBL:EPY86525.1, ECO:0000313|Proteomes:UP000030684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX PubMed=23149746;
RG Bactrian Camels Genome Sequencing and Analysis Consortium;
RA Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA Bayaer T., Li Y., Meng H.;
RT "Genome sequences of wild and domestic bactrian camels.";
RL Nat. Commun. 3:1202-1202(2012).
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; KB016599; EPY86525.1; -; Genomic_DNA.
DR RefSeq; XP_014408409.1; XM_014552923.1.
DR AlphaFoldDB; S9YRE3; -.
DR Proteomes; UP000030684; 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:UP000030684}.
SQ SEQUENCE 329 AA; 35059 MW; 36B87C36ABA28599 CRC64;
MSRVPAFLSA ADVQAHLPSA SLLIPPLEAA LANFSSGPDG GVMQPVRTVM PVAKHRGFLG
VMSAYSAAED ALSTKLITFY EDHSATSPGP SHQATVLLFE PSNGSLLAVM DGNVITAQRT
AAVSAIATKF LKPPSSEVLC ILGAGVQAYS HYEVFTEQFS FKEVRIWNRT KENAEKFADT
VQGEVQVCSS VQEAVAGADV IITVTMATEP ILFGEWVKPG VHINAIGASR PDWRELDDEL
MEEAVLYVDS QEAALKESGD VLLSGAKIFA ELGEVVKGVK PAYCEKTTVF KSLGKSHCSQ
GTALTRAQGM AVEDMVAAKL VYDSWSCGK
//
