ID G7PBJ9_MACFA Unreviewed; 478 AA.
AC G7PBJ9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Retinal dehydrogenase 2 {ECO:0000256|ARBA:ARBA00041052};
DE EC=1.2.1.36 {ECO:0000256|ARBA:ARBA00039134};
DE AltName: Full=Aldehyde dehydrogenase family 1 member A2 {ECO:0000256|ARBA:ARBA00041636};
DE AltName: Full=Retinaldehyde-specific dehydrogenase type 2 {ECO:0000256|ARBA:ARBA00043059};
DE Flags: Fragment;
GN ORFNames=EGM_16011 {ECO:0000313|EMBL:EHH63109.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000313|EMBL:EHH63109.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH63109.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + retinal = 2 H(+) + NADH + retinoate;
CC Xref=Rhea:RHEA:16177, ChEBI:CHEBI:15035, ChEBI:CHEBI:15036,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.36;
CC Evidence={ECO:0000256|ARBA:ARBA00036070};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16178;
CC Evidence={ECO:0000256|ARBA:ARBA00036070};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-13,14-dihydroretinal + H2O + NAD(+) = all-
CC trans-13,14-dihydroretinoate + 2 H(+) + NADH; Xref=Rhea:RHEA:75119,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:194182, ChEBI:CHEBI:194183;
CC Evidence={ECO:0000256|ARBA:ARBA00035998};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75120;
CC Evidence={ECO:0000256|ARBA:ARBA00035998};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2
CC H(+) + NADH; Xref=Rhea:RHEA:42080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.36;
CC Evidence={ECO:0000256|ARBA:ARBA00035919};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42081;
CC Evidence={ECO:0000256|ARBA:ARBA00035919};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000256|ARBA:ARBA00004891}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CM001282; EHH63109.1; -; Genomic_DNA.
DR AlphaFoldDB; G7PBJ9; -.
DR eggNOG; KOG2450; Eukaryota.
DR Proteomes; UP000009130; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd07141; ALDH_F1AB_F2_RALDH1; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR11699:SF102; RETINAL DEHYDROGENASE 2; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 6..469
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 246
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHH63109.1"
SQ SEQUENCE 478 AA; 52384 MW; 069D0F022FA9A956 CRC64;
FINNEWQNSE SGRVFPVYNP ATGEQVCEVQ EADKADIDKA VQAARLAFSL GSVWRRMDAS
ERGRLLDKLA DLVERDRAVL ATMESLNGGK PFLQAFYVDL QGVIKTLRYY AGWADKIHGM
TIPVDGDYFT FTRHEPIGVC GQIIPWNFPL LMFAWKIAPA LCCGNTVVIK PAEQTPLSAL
YMGALIKEAG FPPGVVNILP GYGPTAGAAI ASHIGIDKIA FTGSTEVGKL IQEAAGRSNL
KRVTLELGGK SPNIIFADAD LDYAVEQAHQ GVFFNQGQCC TAGSRIFVEE SIYEEFVRRS
VERAKRRIVG SPFDPTTEQG PQIDKKQYNK ILELIQSGVA EGAKLECGGK GLGRKGFFIE
PTVFSNVTDD MRIAKEEIFG PVQEILRFKT MDEVIERANN SDFGLVAAVF TNDINKALTV
SSAMQAGTVW INCYNALNAQ SPFGGFKMSG NGREMGEFGL REYSEVKTVT VKIPQKNS
//
