ID AL9A1_GADMC Reviewed; 503 AA.
AC P56533;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 22-FEB-2023, entry version 103.
DE RecName: Full=4-trimethylaminobutyraldehyde dehydrogenase;
DE Short=TMABA-DH;
DE Short=TMABADH;
DE EC=1.2.1.47 {ECO:0000250|UniProtKB:P49189};
DE AltName: Full=Aldehyde dehydrogenase family 9 member A1;
DE EC=1.2.1.3 {ECO:0000250|UniProtKB:P49189};
DE AltName: Full=Betaine aldehyde dehydrogenase {ECO:0000303|PubMed:9792097};
DE Short=BADH;
GN Name=aldh9A1;
OS Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8053;
RN [1] {ECO:0007744|PDB:1A4S, ECO:0007744|PDB:1BPW}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
RC TISSUE=Liver;
RX PubMed=9792097; DOI=10.1002/pro.5560071007;
RA Johansson K., El-Ahmad M., Ramaswamy S., Hjelmqvist L., Joernvall H.,
RA Eklund H.;
RT "Structure of betaine aldehyde dehydrogenase at 2.1-A resolution.";
RL Protein Sci. 7:2106-2117(1998).
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. {ECO:0000250|UniProtKB:P49189}.
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:0000250|UniProtKB:P49189};
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:P49189};
CC -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC {ECO:0000250|UniProtKB:P49189}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9792097}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9JLJ3}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally named betaine aldehyde dehydrogenase
CC (PubMed:9792097). Sequence similarity is higher with aldehyde
CC dehydrogenase family 9 member A1, suggesting it has the same function
CC and catalytic activities as other homologs.
CC {ECO:0000303|PubMed:9792097, ECO:0000305}.
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DR PDB; 1A4S; X-ray; 2.10 A; A/B/C/D=1-503.
DR PDB; 1BPW; X-ray; 2.80 A; A/B/C/D=1-503.
DR PDBsum; 1A4S; -.
DR PDBsum; 1BPW; -.
DR AlphaFoldDB; P56533; -.
DR SMR; P56533; -.
DR DIP; DIP-2908N; -.
DR UniPathway; UPA00118; -.
DR EvolutionaryTrace; P56533; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0047105; F:4-trimethylammoniobutyraldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0045329; P:carnitine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07090; ALDH_F9_TMBADH; 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:SF232; 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE A-RELATED; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NAD; Oxidoreductase.
FT CHAIN 1..503
FT /note="4-trimethylaminobutyraldehyde dehydrogenase"
FT /id="PRO_0000056532"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 297
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:9792097,
FT ECO:0007744|PDB:1BPW"
FT BINDING 241..245
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:9792097,
FT ECO:0007744|PDB:1BPW"
FT BINDING 400
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:9792097,
FT ECO:0007744|PDB:1BPW"
FT SITE 166
FT /note="Transition state stabilizer"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:1A4S"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1A4S"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 79..95
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 112..132
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 196..207
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:1A4S"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 310..322
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 342..358
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 403..411
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 437..446
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 449..455
FT /evidence="ECO:0007829|PDB:1A4S"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:1BPW"
FT HELIX 481..485
FT /evidence="ECO:0007829|PDB:1A4S"
FT STRAND 486..494
FT /evidence="ECO:0007829|PDB:1A4S"
SQ SEQUENCE 503 AA; 54368 MW; 1CB2FB92FA89E577 CRC64;
AQLVDSMPSA STGSVVVTDD LNYWGGRRIK SKDGATTEPV FEPATGRVLC QMVPCGAEEV
DQAVQSAQAA YLKWSKMAGI ERSRVMLEAA RIIRERRDNI AKLEVINNGK TITEAEYDID
AAWQCIEYYA GLAPTLSGQH IQLPGGAFAY TRREPLGVCA GILAWNYPFM IAAWKCAPAL
ACGNAVVFKP SPMTPVTGVI LAEIFHEAGV PVGLVNVVQG GAETGSLLCH HPNVAKVSFT
GSVPTGKKVM EMSAKTVKHV TLELGGKSPL LIFKDCELEN AVRGALMANF LTQGQVCTNG
TRVFVQREIM PQFLEEVVKR TKAIVVGDPL LTETRMGGLI SKPQLDKVLG FVAQAKKEGA
RVLCGGEPLT PSDPKLKNGY FMSPCVLDNC RDDMTCVKEE IFGPVMSVLP FDTEEEVLQR
ANNTTFGLAS GVFTRDISRA HRVAANLEAG TCYINTYSIS PVEVPFGGYK MSGFGRENGQ
ATVDYYSQLK TVIVEMGDVD SLF
//
