ADH1B_MAIZE
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 03-AUG-2022, entry version 41.
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 SMR; G5DDC2; -.
DR STRING; 4577.GRMZM2G016189_P02; -.
DR GeneID; 606443; -.
DR KEGG; zma:606443; -.
DR eggNOG; KOG2450; Eukaryota.
DR OMA; EGGHYSF; -.
DR OrthoDB; 153834at2759; -.
DR BRENDA; 1.2.1.19; 6752.
DR BRENDA; 1.2.1.8; 6752.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000007305; Chromosome 1.
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 Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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 Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 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
