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}. 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 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 //