ID A9V9Q9_MONBE Unreviewed; 864 AA.
AC A9V9Q9;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
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=MONBRDRAFT_34126 {ECO:0000313|EMBL:EDQ85766.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ85766.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ85766.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
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 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009463}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CH991571; EDQ85766.1; -; Genomic_DNA.
DR RefSeq; XP_001749481.1; XM_001749429.1.
DR AlphaFoldDB; A9V9Q9; -.
DR STRING; 81824.A9V9Q9; -.
DR EnsemblProtists; EDQ85766; EDQ85766; MONBRDRAFT_34126.
DR GeneID; 5894683; -.
DR KEGG; mbr:MONBRDRAFT_34126; -.
DR eggNOG; KOG2304; Eukaryota.
DR eggNOG; KOG2450; Eukaryota.
DR InParanoid; A9V9Q9; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0047105; F:4-trimethylammoniobutyraldehyde dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11699:SF228; 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00067; 3HCDH; 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:UP000001357}.
FT DOMAIN 48..506
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 577..763
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 765..862
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT ACT_SITE 277
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 864 AA; 93678 MW; FD02D49F51F6C95E CRC64;
MLERALCARH ALGQGLKAHL DGFQLLRAPV VTSFINGRYI EPTNDPSRDM HWIEPATKQA
HVRVEAAAMA DLDEALQGAQ AAQQQWALTS GMERARALMD VAHYLRTHTT ACESIECLDT
GRPFREMALA DLPSVIDSFE YFAGVAQRVS GEHYDMGGGS FAYTRREPLG ICAGIGAWNY
PMQGAAWKAA PAMATGNALV FKPSEHTPLS ALLLAEAVQQ VEAIPTGLFN VVLGDGALGA
TFATNPSFAK VSFTGSRATG LKITSAAAGD LKRVTMELGG KSPLIICADA DLEQACRGAI
MANFFSNGQV CSNGTRVFVA REVYQPFTQR LVELTAQLRA GDSFDEQVAV TPVIHNDHAA
RVREFLERAR TQGATVLYGG EYADEEVPSH IDRTGLIKPH ILTDCSDDME IVREEVFGPV
MAVLPFDTVD EAVRRANDTP YGLSAGVFTQ DLKQAHRVIA ELKAGTTWIN DYNLAPTQLP
WGGYKQSGVG RENGTDAINH WTQLKRIGSR ERAKRERERD LLFSGHCFLF LSLSFSLFLS
LSEDNGNDKM MAAMVPRAPV LAGRALSTAT ARHNISHVTV IGGGLMGSGI AQVAAGSQHK
VVLCDVSQDV LDKTINRIET SLGRVAKKKF ADDANGAKDF IAATMDNLST STDAVKTIGD
GTDLVVEAIK EDLDLKKKVF AEYDAVAKDH TIFASNTSSL SIGKIAEATQ RKDRFGGLHF
FNPVPVMKLV EVIRISETSD ETFQALKSFG EAVGKHVVVC KDTPGFIVNR LLVPYLLEAA
RMVERGDATI EDVDAAMKLG AGYPMGPFQL LDYVGLDTTA FIAQGWAEDY PEEPLFKPVN
VIAEKVKEGK LGNKSGQGFY DYSK
//
