ABDH_ECOLI
ID ABDH_ECOLI Reviewed; 474 AA.
AC P77674;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Gamma-aminobutyraldehyde dehydrogenase {ECO:0000303|PubMed:16023116, ECO:0000303|PubMed:3510672};
DE Short=ABALDH {ECO:0000303|PubMed:16023116};
DE EC=1.2.1.19 {ECO:0000269|PubMed:16023116, ECO:0000269|PubMed:3510672};
DE AltName: Full=1-pyrroline dehydrogenase;
DE AltName: Full=4-aminobutanal dehydrogenase;
DE AltName: Full=5-aminopentanal dehydrogenase {ECO:0000305|PubMed:30498244};
DE EC=1.2.1.- {ECO:0000269|PubMed:30498244, ECO:0000305|PubMed:28522202};
GN Name=patD {ECO:0000303|PubMed:22636776}; Synonyms=prr, ydcW;
GN OrderedLocusNames=b1444, JW1439;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=3510672; DOI=10.1016/0304-4165(86)90085-1;
RA Prieto-Santos M.I., Martin-Checa J., Balana-Fouce R., Garrido-Pertierra A.;
RT "A pathway for putrescine catabolism in Escherichia coli.";
RL Biochim. Biophys. Acta 880:242-244(1986).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT,
RP INDUCTION, AND KINETIC PARAMETERS.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16023116; DOI=10.1016/j.febslet.2005.06.038;
RA Samsonova N.N., Smirnov S.V., Novikova A.E., Ptitsyn L.R.;
RT "Identification of Escherichia coli K12 YdcW protein as a gamma-
RT aminobutyraldehyde dehydrogenase.";
RL FEBS Lett. 579:4107-4112(2005).
RN [6]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=22636776; DOI=10.1128/jb.05063-11;
RA Schneider B.L., Reitzer L.;
RT "Pathway and enzyme redundancy in putrescine catabolism in Escherichia
RT coli.";
RL J. Bacteriol. 194:4080-4088(2012).
RN [7]
RP BIOTECHNOLOGY, AND CATALYTIC ACTIVITY.
RX PubMed=28522202; DOI=10.1016/j.biortech.2017.04.108;
RA Jorge J.M.P., Perez-Garcia F., Wendisch V.F.;
RT "A new metabolic route for the fermentative production of 5-aminovalerate
RT from glucose and alternative carbon sources.";
RL Bioresour. Technol. 245:1701-1709(2017).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=30498244; DOI=10.1038/s41467-018-07563-6;
RA Knorr S., Sinn M., Galetskiy D., Williams R.M., Wang C., Mueller N.,
RA Mayans O., Schleheck D., Hartig J.S.;
RT "Widespread bacterial lysine degradation proceeding via glutarate and L-2-
RT hydroxyglutarate.";
RL Nat. Commun. 9:5071-5071(2018).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH NAD
RP AND BETAINE ALDEHYDE, FUNCTION, AND SUBUNIT.
RX PubMed=15381418; DOI=10.1016/j.jmb.2004.08.030;
RA Gruez A., Roig-Zamboni V., Grisel S., Salomoni A., Valencia C.,
RA Campanacci V., Tegoni M., Cambillau C.;
RT "Crystal structure and kinetics identify Escherichia coli YdcW gene product
RT as a medium-chain aldehyde dehydrogenase.";
RL J. Mol. Biol. 343:29-41(2004).
CC -!- FUNCTION: Catalyzes the oxidation 4-aminobutanal (gamma-
CC aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA)
CC (PubMed:3510672, PubMed:16023116). This is the second step in one of
CC two pathways for putrescine degradation, where putrescine is converted
CC into 4-aminobutanoate via 4-aminobutanal, which allows E.coli to grow
CC on putrescine as the sole nitrogen source (PubMed:3510672,
CC PubMed:22636776). Also functions as a 5-aminopentanal dehydrogenase in
CC a a L-lysine degradation pathway to succinate that proceeds via
CC cadaverine, glutarate and L-2-hydroxyglutarate (PubMed:30498244). Can
CC also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic
CC efficiency (PubMed:15381418, PubMed:16023116).
CC {ECO:0000269|PubMed:15381418, ECO:0000269|PubMed:16023116,
CC ECO:0000269|PubMed:22636776, ECO:0000269|PubMed:30498244,
CC ECO:0000269|PubMed:3510672}.
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:16023116, ECO:0000269|PubMed:3510672};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC Evidence={ECO:0000305|PubMed:3510672};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-aminopentanal + H2O + NAD(+) = 5-aminopentanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:61632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:144896,
CC ChEBI:CHEBI:356010; Evidence={ECO:0000269|PubMed:30498244,
CC ECO:0000305|PubMed:28522202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61633;
CC Evidence={ECO:0000305|PubMed:30498244};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=41 uM for 4-aminobutanal {ECO:0000269|PubMed:16023116};
CC KM=196 uM for butanal {ECO:0000269|PubMed:16023116};
CC KM=54 uM for NAD(+) {ECO:0000269|PubMed:16023116};
CC KM=484 uM for NADP(+) {ECO:0000269|PubMed:16023116};
CC KM=18 uM for 1-pyrroline {ECO:0000269|PubMed:3510672};
CC KM=37 uM for NAD(+) {ECO:0000269|PubMed:3510672};
CC Vmax=9.08 umol/min/mg enzyme with 4-aminobutanal as substrate
CC {ECO:0000269|PubMed:16023116};
CC Vmax=0.36 umol/min/mg enzyme with butanal as substrate
CC {ECO:0000269|PubMed:16023116};
CC pH dependence:
CC Optimum pH is 5.4. {ECO:0000269|PubMed:3510672};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4-
CC aminobutanoate from 4-aminobutanal: step 1/1.
CC {ECO:0000269|PubMed:22636776, ECO:0000269|PubMed:3510672}.
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000305|PubMed:30498244}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15381418,
CC ECO:0000269|PubMed:16023116}.
CC -!- INDUCTION: Up-regulated under nitrogen starvation conditions.
CC {ECO:0000269|PubMed:16023116}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a high decrease in
CC gamma-aminobutyraldehyde dehydrogenase activity, but are still able to
CC grow with putrescine as the sole nitrogen source. However, a mutant
CC lacking both patD and puuC cannot grow with putrescine as the sole
CC nitrogen source. {ECO:0000269|PubMed:22636776}.
CC -!- BIOTECHNOLOGY: Can be used in the industrial production of the value-
CC added compound 5-aminovalerate. {ECO:0000269|PubMed:28522202}.
CC -!- MISCELLANEOUS: 4-aminobutanal can spontaneously cyclize to 1-pyrroline,
CC and 5-aminopentanal to 1-piperideine. {ECO:0000269|PubMed:30498244,
CC ECO:0000269|PubMed:3510672}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. Gamma-
CC aminobutyraldehyde dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC74526.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15073.1; -; Genomic_DNA.
DR PIR; G64896; G64896.
DR RefSeq; NP_415961.1; NC_000913.3.
DR RefSeq; WP_001163872.1; NZ_LN832404.1.
DR PDB; 1WNB; X-ray; 2.20 A; A/B/C/D=1-474.
DR PDB; 1WND; X-ray; 2.10 A; A/B/C/D=1-474.
DR PDBsum; 1WNB; -.
DR PDBsum; 1WND; -.
DR AlphaFoldDB; P77674; -.
DR SMR; P77674; -.
DR BioGRID; 4260192; 6.
DR DIP; DIP-11656N; -.
DR IntAct; P77674; 4.
DR STRING; 511145.b1444; -.
DR DrugBank; DB04401; Betaine aldehyde.
DR jPOST; P77674; -.
DR PaxDb; P77674; -.
DR PRIDE; P77674; -.
DR EnsemblBacteria; AAC74526; AAC74526; b1444.
DR EnsemblBacteria; BAA15073; BAA15073; BAA15073.
DR GeneID; 945876; -.
DR KEGG; ecj:JW1439; -.
DR KEGG; eco:b1444; -.
DR PATRIC; fig|1411691.4.peg.824; -.
DR EchoBASE; EB3529; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_6; -.
DR InParanoid; P77674; -.
DR OMA; NDDLGEV; -.
DR PhylomeDB; P77674; -.
DR BioCyc; EcoCyc:G6755-MON; -.
DR BioCyc; MetaCyc:G6755-MON; -.
DR BRENDA; 1.2.1.19; 2026.
DR SABIO-RK; P77674; -.
DR UniPathway; UPA00188; UER00292.
DR EvolutionaryTrace; P77674; -.
DR PRO; PR:P77674; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0033737; F:1-pyrroline dehydrogenase activity; IMP:EcoCyc.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:EcoCyc.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019477; P:L-lysine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009447; P:putrescine catabolic process; IMP:EcoCyc.
DR CDD; cd07092; ALDH_ABALDH-YdcW; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR HAMAP; MF_01275; Aldedh_Prr; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR015657; Aminobutyraldehyde_DH.
DR InterPro; IPR017749; PatD.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR03374; ABALDH; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..474
FT /note="Gamma-aminobutyraldehyde dehydrogenase"
FT /id="PRO_0000056563"
FT ACT_SITE 246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 280
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT BINDING 146..148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15381418,
FT ECO:0007744|PDB:1WNB"
FT BINDING 172..175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15381418,
FT ECO:0007744|PDB:1WNB"
FT BINDING 209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15381418,
FT ECO:0007744|PDB:1WNB"
FT BINDING 225..228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15381418,
FT ECO:0007744|PDB:1WNB"
FT BINDING 280
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15381418,
FT ECO:0007744|PDB:1WNB"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:1WND"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 38..55
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 60..76
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:1WND"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1WND"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:1WND"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 325..340
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 381..389
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 392..400
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 415..424
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:1WND"
FT HELIX 457..462
FT /evidence="ECO:0007829|PDB:1WND"
FT STRAND 465..473
FT /evidence="ECO:0007829|PDB:1WND"
SQ SEQUENCE 474 AA; 50830 MW; 487C6044719A41E3 CRC64;
MQHKLLINGE LVSGEGEKQP VYNPATGDVL LEIAEASAEQ VDAAVRAADA AFAEWGQTTP
KVRAECLLKL ADVIEENGQV FAELESRNCG KPLHSAFNDE IPAIVDVFRF FAGAARCLNG
LAAGEYLEGH TSMIRRDPLG VVASIAPWNY PLMMAAWKLA PALAAGNCVV LKPSEITPLT
ALKLAELAKD IFPAGVINIL FGRGKTVGDP LTGHPKVRMV SLTGSIATGE HIISHTASSI
KRTHMELGGK APVIVFDDAD IEAVVEGVRT FGYYNAGQDC TAACRIYAQK GIYDTLVEKL
GAAVATLKSG APDDESTELG PLSSLAHLER VGKAVEEAKA TGHIKVITGG EKRKGNGYYY
APTLLAGALQ DDAIVQKEVF GPVVSVTPFD NEEQVVNWAN DSQYGLASSV WTKDVGRAHR
VSARLQYGCT WVNTHFMLVS EMPHGGQKLS GYGKDMSLYG LEDYTVVRHV MVKH
