ID ADH1B_MAIZE Reviewed; 506 AA. AC G5DDC2; A0A1D6KPH6; Q53CF4; DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot. DT 14-DEC-2011, sequence version 1. DT 27-MAR-2024, entry version 47. DE RecName: Full=Aminoaldehyde dehydrogenase 1b {ECO:0000303|PubMed:23408433}; DE Short=ZmAMADH1b {ECO:0000303|PubMed:23408433}; DE EC=1.2.1.- {ECO:0000269|PubMed:23408433}; DE AltName: Full=4-trimethylammoniobutyraldehyde dehydrogenase AMADH1b {ECO:0000305}; DE EC=1.2.1.47 {ECO:0000269|PubMed:23408433}; DE AltName: Full=Aminobutyraldehyde dehydrogenase AMADH1b {ECO:0000305}; DE EC=1.2.1.19 {ECO:0000269|PubMed:23408433}; DE AltName: Full=Betaine aldehyde dehydrogenase AMADH1b {ECO:0000305}; DE EC=1.2.1.8 {ECO:0000269|PubMed:23408433}; DE AltName: Full=Gamma-guanidinobutyraldehyde dehydrogenase AMADH1b {ECO:0000305}; DE EC=1.2.1.54 {ECO:0000269|PubMed:23408433}; GN Name=AMADH1B {ECO:0000303|PubMed:23408433}; GN Synonyms=ALDH10A9 {ECO:0000303|PubMed:23408433}; GN ORFNames=ZEAMMB73_Zm00001d032257 {ECO:0000312|EMBL:ONM04709.1}; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC TISSUE=Meristem; RX PubMed=23408433; DOI=10.1074/jbc.m112.443952; RA Kopecny D., Koncitikova R., Tylichova M., Vigouroux A., Moskalikova H., RA Soural M., Sebela M., Morera S.; RT "Plant ALDH10 family: identifying critical residues for substrate RT specificity and trapping a thiohemiacetal intermediate."; RL J. Biol. Chem. 288:9491-9507(2013). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Aili Y., Jingsheng X., Rukai C.; RT "Cloning and Sequencing of BADH Gene from Zea mays."; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. B73; RX PubMed=19965430; DOI=10.1126/science.1178534; RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S., RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D., RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K., RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M., RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B., RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E., RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J., RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E., RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A., RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R., RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A., RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E., RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A., RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T., RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L., RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P., RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A., RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C., RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A., RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C., RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W., RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C., RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K., RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K., RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S., RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.; RT "The B73 maize genome: complexity, diversity, and dynamics."; RL Science 326:1112-1115(2009). CC -!- FUNCTION: Dehydrogenase that catalyzes the oxidation of several CC aminoaldehydes (PubMed:23408433). Metabolizes and detoxifies aldehyde CC products of polyamine degradation to non-toxic amino acids (Probable). CC Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4- CC aminobutanoate and beta-alanine, respectively (PubMed:23408433). CC Catalyzes the oxidation of 4-(trimethylamino)butanal and 4- CC guanidinobutanal to 4-trimethylammoniobutanoate and 4- CC guanidinobutanoate, respectively (PubMed:23408433). Catalyzes the CC oxidation of betaine aldehyde to glycine betaine (PubMed:23408433). CC {ECO:0000269|PubMed:23408433, ECO:0000305}. 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:0000269|PubMed:23408433}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106; CC Evidence={ECO:0000269|PubMed:23408433}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-aminopropanal + H2O + NAD(+) = beta-alanine + 2 H(+) + NADH; CC Xref=Rhea:RHEA:30695, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57966, CC ChEBI:CHEBI:58374; Evidence={ECO:0000269|PubMed:23408433}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696; CC Evidence={ECO:0000269|PubMed:23408433}; 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:0000269|PubMed:23408433}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17986; CC Evidence={ECO:0000269|PubMed:23408433}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-guanidinobutanal + H2O + NAD(+) = 4-guanidinobutanoate + 2 CC H(+) + NADH; Xref=Rhea:RHEA:14381, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57486, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57854, ChEBI:CHEBI:57945; EC=1.2.1.54; CC Evidence={ECO:0000269|PubMed:23408433}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14382; CC Evidence={ECO:0000269|PubMed:23408433}; CC -!- CATALYTIC ACTIVITY: CC Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + CC NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; EC=1.2.1.8; CC Evidence={ECO:0000269|PubMed:23408433}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306; CC Evidence={ECO:0000269|PubMed:23408433}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=26 uM for 4-aminobutanal {ECO:0000269|PubMed:23408433}; CC KM=11 uM for 3-aminopropanal {ECO:0000269|PubMed:23408433}; CC KM=10 uM for 4-(trimethylamino)butanal {ECO:0000269|PubMed:23408433}; CC KM=5 uM for 4-guanidinobutanal {ECO:0000269|PubMed:23408433}; CC KM=29 uM for betaine aldehyde {ECO:0000269|PubMed:23408433}; CC KM=79 uM for NAD(+) with 3-aminopropanal as substrate CC {ECO:0000269|PubMed:23408433}; CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via CC choline pathway; betaine from betaine aldehyde: step 1/1. CC {ECO:0000305}. 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; JN635700; AEP68091.1; -; mRNA. DR EMBL; AY587278; AAT70230.1; -; mRNA. DR EMBL; CM007647; ONM04709.1; -; Genomic_DNA. DR RefSeq; NP_001105781.1; NM_001112311.1. DR AlphaFoldDB; G5DDC2; -. DR SMR; G5DDC2; -. DR IntAct; G5DDC2; 3. DR STRING; 4577.A0A1D6KPH6; -. DR PaxDb; 4577-GRMZM2G016189_P02; -. DR GeneID; 606443; -. DR KEGG; zma:606443; -. DR eggNOG; KOG2450; Eukaryota. DR InParanoid; G5DDC2; -. DR OMA; EFYAGAC; -. DR OrthoDB; 3078548at2759; -. DR BRENDA; 1.2.1.19; 6752. DR BRENDA; 1.2.1.8; 6752. DR UniPathway; UPA00529; UER00386. DR Proteomes; UP000007305; Unplaced. DR GO; GO:0033737; F:1-pyrroline dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0047105; F:4-trimethylammoniobutyraldehyde dehydrogenase activity; IDA:UniProtKB. DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IDA:UniProtKB. DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IDA:UniProtKB. DR GO; GO:0047107; F:gamma-guanidinobutyraldehyde dehydrogenase activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0031402; F:sodium ion binding; ISS:UniProtKB. DR GO; GO:0110095; P:cellular detoxification of aldehyde; IDA:UniProtKB. DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway. DR CDD; cd07110; ALDH_F10_BADH; 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; PTHR43860; BETAINE ALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR43860:SF2; BETAINE 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 Metal-binding; NAD; Oxidoreductase; Reference proteome; Sodium. FT CHAIN 1..506 FT /note="Aminoaldehyde dehydrogenase 1b" FT /id="PRO_0000454136" 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 102 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000250|UniProtKB:C0P9J6" FT BINDING 162..164 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:C0P9J6" FT BINDING 188..191 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:C0P9J6" FT BINDING 192 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000250|UniProtKB:C0P9J6" FT BINDING 242..245 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:C0P9J6" FT BINDING 263 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:C0P9J6" FT BINDING 396 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:C0P9J6" FT BINDING 462 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:C0P9J6" FT SITE 165 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P20000" FT CONFLICT 1 FT /note="Missing (in Ref. 2; AAT70230)" FT /evidence="ECO:0000305" FT CONFLICT 312..316 FT /note="EFNEK -> KFNER (in Ref. 2; AAT70230)" FT /evidence="ECO:0000305" SQ SEQUENCE 506 AA; 55080 MW; 52E9E0CEEC55E3A0 CRC64; MMASQAMVPL RQLFVDGEWR PPAQGRRLPV VNPTTEAHIG EIPAGTAEDV DAAVAAARAA LKRNRGRDWA RAPGAVRAKY LRAIAAKVIE RKQELAKLEA LDCGKPYDEA AWDMDDVAGC FEYFADQAEA LDKRQNSPVS LPMETFKCHL RREPIGVVGL ITPWNYPLLM ATWKVAPALA AGCAAVLKPS ELASVTCLEL ADICKEVGLP PGVLNIVTGL GPDAGAPLSA HPDVDKVAFT GSFETGKKIM AAAAPMVKPV TLELGGKSPI VVFDDVDIDK AVEWTLFGCF WTNGQICSAT SRLLVHTKIA KEFNEKMVAW AKNIKVSDPL EEGCRLGPVV SEGQYEKIKK FILNAKSEGA TILTGGVRPA HLEKGFFIEP TIITDITTSM EIWREEVFGP VLCVKEFSTE DEAIELANDT QYGLAGAVIS GDRERCQRLS EEIDAGIIWV NCSQPCFCQA PWGGNKRSGF GRELGEGGID NYLSVKQVTE YISDEPWGWY RSPSKL //