AL3A2_PONAB
ID AL3A2_PONAB Reviewed; 485 AA.
AC Q5RF60;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Aldehyde dehydrogenase family 3 member A2;
DE EC=1.2.1.3 {ECO:0000250|UniProtKB:P51648};
DE EC=1.2.1.94 {ECO:0000250|UniProtKB:P51648};
DE AltName: Full=Fatty aldehyde dehydrogenase;
GN Name=ALDH3A2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of medium and long-chain aliphatic
CC aldehydes to fatty acids. Active on a variety of saturated and
CC unsaturated aliphatic aldehydes between 6 and 24 carbons in length.
CC Responsible for conversion of the sphingosine 1-phosphate (S1P)
CC degradation product hexadecenal to hexadecenoic acid.
CC {ECO:0000250|UniProtKB:P51648}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty aldehyde + H2O + NAD(+) = a fatty acid + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:49832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:35746, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexadecenal + H2O + NAD(+) = (E)-hexadec-2-enoate + 2
CC H(+) + NADH; Xref=Rhea:RHEA:36135, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17585, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:72745;
CC Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoate + NADH = H2O + hexadecanal + NAD(+);
CC Xref=Rhea:RHEA:33739, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17600, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=22-oxodocosanoate + H2O + NAD(+) = docosanedioate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:39015, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76298,
CC ChEBI:CHEBI:76299; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,6,10,14-tetramethylpentadecanal + H2O + NAD(+) = 2,6,10,14-
CC tetramethylpentadecanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:44016,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:49189,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:77268;
CC Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + octadecanal = 2 H(+) + NADH + octadecanoate;
CC Xref=Rhea:RHEA:44020, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17034, ChEBI:CHEBI:25629, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoate + 2 H(+) + NADH = dodecanal + H2O + NAD(+);
CC Xref=Rhea:RHEA:44168, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:27836, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanal + H2O + NAD(+) = decanoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:44104, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27689, ChEBI:CHEBI:31457, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + tetradecanal = 2 H(+) + NADH + tetradecanoate;
CC Xref=Rhea:RHEA:44172, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:84067; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate;
CC Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + heptanal + NAD(+) = 2 H(+) + heptanoate + NADH;
CC Xref=Rhea:RHEA:44108, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32362, ChEBI:CHEBI:34787, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesal + H2O + NAD(+) = (2E,6E)-farnesoate + 2 H(+)
CC + NADH; Xref=Rhea:RHEA:24216, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15894, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:83276; EC=1.2.1.94;
CC Evidence={ECO:0000250|UniProtKB:P51648};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P51648}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:P51648}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P51648}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P51648}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P51648}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P30839}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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; CR857301; CAH89597.1; -; mRNA.
DR RefSeq; NP_001124709.1; NM_001131237.2.
DR AlphaFoldDB; Q5RF60; -.
DR SMR; Q5RF60; -.
DR STRING; 9601.ENSPPYP00000023716; -.
DR Ensembl; ENSPPYT00000055044; ENSPPYP00000039570; ENSPPYG00000008838.
DR GeneID; 100171557; -.
DR KEGG; pon:100171557; -.
DR CTD; 224; -.
DR eggNOG; KOG2456; Eukaryota.
DR GeneTree; ENSGT00940000157944; -.
DR InParanoid; Q5RF60; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0050061; F:long-chain-aldehyde dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0052814; F:medium-chain-aldehyde dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046458; P:hexadecanal metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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 InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; PTHR43570; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Fatty acid metabolism; Lipid metabolism; Membrane;
KW Microsome; NAD; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..485
FT /note="Aldehyde dehydrogenase family 3 member A2"
FT /id="PRO_0000342181"
FT TOPO_DOM 1..463
FT /note="Cytoplasmic"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 481..484
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
FT ACT_SITE 207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 185..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51648"
SQ SEQUENCE 485 AA; 54866 MW; 2DBB29DC3074C3BC CRC64;
MELEVRRVRQ AFLSGRSRPL RFRLQQLEAL RRMVQEREKD ILAAIAADLC KSEFNVYSQE
VITVLGEIDF MLENLPEWVT AKPVKKNVLT MLDEAYIQPQ PLGVVLIIGA WNYPFVLTIQ
PLIGAIAAGN AVIIKPSELS ENTAKMLAKL LPQYLDQDLY IVINGGVEET TELLKQRFDH
IFYTGNTAVG KIVMEAAAKH LTPVTLELGG KSPCYIDKDC DLDIVCRRIT WGKYMNCGQT
CIAPDYILCE ASLQNQIVWK IKETVKEFYG ENIKESPDYE RIINLRHFKR ILSLLEGQKI
AFGGETDEAT RYIAPTVLTD VDPKTKVMQE EIFGPILPIV PVKNVDEAIN FINEREKPLA
LYVFSHNHKL IKRMIDETSS GGVTGNDVIM HFMLNSFPFG GVGSSGMGAY HGKHSFDTFS
HQRPCLLKSL KREGANKLRY PPNSQSKVDW GKFFLLKRFN KEKLGLLLLT FLGIVAAVLV
KAEYY
