ID A0A0D2VGD4_CAPO3 Unreviewed; 533 AA.
AC A0A0D2VGD4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=4-trimethylaminobutyraldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00040275};
DE EC=1.2.1.19 {ECO:0000256|ARBA:ARBA00039138};
DE EC=1.2.1.46 {ECO:0000256|ARBA:ARBA00044057};
DE EC=1.2.1.47 {ECO:0000256|ARBA:ARBA00039125};
DE AltName: Full=Aldehyde dehydrogenase family 9 member A1 {ECO:0000256|ARBA:ARBA00041858};
DE AltName: Full=Formaldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00044324};
DE AltName: Full=Gamma-aminobutyraldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00044302};
GN ORFNames=CAOG_000500 {ECO:0000313|EMBL:KJE88932.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE88932.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts gamma-trimethylaminobutyraldehyde into gamma-
CC butyrobetaine with high efficiency (in vitro). Can catalyze the
CC irreversible oxidation of a broad range of aldehydes to the
CC corresponding acids in an NAD-dependent reaction, but with low
CC efficiency. Catalyzes the oxidation of aldehydes arising from biogenic
CC amines and polyamines. {ECO:0000256|ARBA:ARBA00043882}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5-hydroxyindol-3-yl)acetaldehyde + H2O + NAD(+) = (5-
CC hydroxyindol-3-yl)acetate + 2 H(+) + NADH; Xref=Rhea:RHEA:31215,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:50157,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62622;
CC Evidence={ECO:0000256|ARBA:ARBA00043724};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxyphenylacetaldehyde + H2O + NAD(+) = 3,4-
CC dihydroxyphenylacetate + 2 H(+) + NADH; Xref=Rhea:RHEA:69080,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17612,
CC ChEBI:CHEBI:27978, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000256|ARBA:ARBA00043811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-(trimethylamino)butanal + H2O + NAD(+) = 4-
CC (trimethylamino)butanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:17985,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16244,
CC ChEBI:CHEBI:18020, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.47;
CC Evidence={ECO:0000256|ARBA:ARBA00036400};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264,
CC ChEBI:CHEBI:59888; EC=1.2.1.19;
CC Evidence={ECO:0000256|ARBA:ARBA00043799};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + pentanal = 2 H(+) + NADH + pentanoate;
CC Xref=Rhea:RHEA:69092, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31011, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:84069; Evidence={ECO:0000256|ARBA:ARBA00043741};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate;
CC Xref=Rhea:RHEA:67256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17153, ChEBI:CHEBI:17272, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00043823};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + spermine monoaldehyde = 2 H(+) + N-(2-
CC carboxyethyl)spermidine + NADH; Xref=Rhea:RHEA:69168,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:180903, ChEBI:CHEBI:180913;
CC Evidence={ECO:0000256|ARBA:ARBA00043708};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH;
CC Xref=Rhea:RHEA:67276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:88528; Evidence={ECO:0000256|ARBA:ARBA00043662};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + imidazole-4-acetaldehyde + NAD(+) = 2 H(+) + imidazole-
CC 4-acetate + NADH; Xref=Rhea:RHEA:31059, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27398, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:57969;
CC Evidence={ECO:0000256|ARBA:ARBA00043820};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:25294, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00043790};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acrolein + H2O + NAD(+) = acrylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:69084, ChEBI:CHEBI:15368, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:37080, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00043666};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanal + H2O + NAD(+) = butanoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:69088, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15743, ChEBI:CHEBI:17968, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00043754};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formaldehyde + H2O + NAD(+) = formate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16425, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16842, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.46;
CC Evidence={ECO:0000256|ARBA:ARBA00043759};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; KE346360; KJE88932.1; -; Genomic_DNA.
DR RefSeq; XP_004365371.1; XM_004365314.2.
DR AlphaFoldDB; A0A0D2VGD4; -.
DR STRING; 595528.A0A0D2VGD4; -.
DR EnsemblProtists; KJE88932; KJE88932; CAOG_000500.
DR GeneID; 14902204; -.
DR eggNOG; KOG2450; Eukaryota.
DR InParanoid; A0A0D2VGD4; -.
DR OMA; CREGIRM; -.
DR OrthoDB; 2291791at2759; -.
DR PhylomeDB; A0A0D2VGD4; -.
DR Proteomes; UP000008743; Unassembled WGS sequence.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
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:SF228; 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000008743}.
FT DOMAIN 54..522
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 288
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 533 AA; 56923 MW; 75ADE9B00417B0F7 CRC64;
MLQSVVVRLQ PSASSALSAS VCRRMASSTA LPIITSYING ARVPVDAARA ALCFDKRNPA
TGQVFAQVQS ADERELNHAV AVAQAAQREW AALNGAERSR ILRKAAQLIR DRTQALAEVE
VRDVGKPIAE ALSYDINSGA DVFEYYASVA ATMHGKFFSN FSTSVASRPA RSFAYTIREP
LGVCAGIGAW NYPFQIASWK TAPALACGNS MVFKPSELTP SSAVELAAIL TEAGVPAGVF
NVVQGAGNIG RGITAHPDIA KVTFTGESGT GKHVMRSSSD SLKKVTLELG GKSPLIVFDD
CKLDDAVSGA LMANFYTQGE VCTNGTRVFV QRSIHDKFIA RLRERMSATA QPGIVIGNPM
DEKTNVGALI SEPHMQKVLG YIAKGKAEGA KLIAGGNRFQ PTDAAFKDGY FVEPTVFDEC
SDSMAIVREE IFGPVMSILP FDTDEEVIRR ANATSFGLAA GVFTSSLQRA HTSVASLQAG
IVWVNNYNLA PVEVPFGGFK ESGIGKENGT ESIENFTQLK MVYMEMDGIA SVF
//
