ABDH_ECODH
ID ABDH_ECODH Reviewed; 474 AA.
AC B1XDF5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Gamma-aminobutyraldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01275};
DE Short=ABALDH {ECO:0000255|HAMAP-Rule:MF_01275};
DE EC=1.2.1.19 {ECO:0000255|HAMAP-Rule:MF_01275};
DE AltName: Full=1-pyrroline dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01275};
DE AltName: Full=4-aminobutanal dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01275};
DE AltName: Full=5-aminopentanal dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01275};
DE EC=1.2.1.- {ECO:0000255|HAMAP-Rule:MF_01275};
GN Name=patD {ECO:0000255|HAMAP-Rule:MF_01275};
GN OrderedLocusNames=ECDH10B_1574;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
CC -!- FUNCTION: Catalyzes the oxidation 4-aminobutanal (gamma-
CC aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA).
CC This is the second step in one of two pathways for putrescine
CC degradation, where putrescine is converted into 4-aminobutanoate via 4-
CC aminobutanal. Also functions as a 5-aminopentanal dehydrogenase in a a
CC L-lysine degradation pathway to succinate that proceeds via cadaverine,
CC glutarate and L-2-hydroxyglutarate. {ECO:0000255|HAMAP-Rule:MF_01275}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01275};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01275};
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:0000255|HAMAP-Rule:MF_01275};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61633;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01275};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4-
CC aminobutanoate from 4-aminobutanal: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01275}.
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000255|HAMAP-Rule:MF_01275}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01275}.
CC -!- MISCELLANEOUS: 4-aminobutanal can spontaneously cyclize to 1-pyrroline,
CC and 5-aminopentanal to 1-piperideine. {ECO:0000255|HAMAP-
CC Rule:MF_01275}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. Gamma-
CC aminobutyraldehyde dehydrogenase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01275}.
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; CP000948; ACB02660.1; -; Genomic_DNA.
DR RefSeq; WP_001163872.1; NC_010473.1.
DR AlphaFoldDB; B1XDF5; -.
DR SMR; B1XDF5; -.
DR KEGG; ecd:ECDH10B_1574; -.
DR HOGENOM; CLU_005391_1_0_6; -.
DR OMA; NDDLGEV; -.
DR BioCyc; ECOL316385:ECDH10B_RS08075-MON; -.
DR UniPathway; UPA00188; UER00292.
DR GO; GO:0033737; F:1-pyrroline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW NAD; Oxidoreductase.
FT CHAIN 1..474
FT /note="Gamma-aminobutyraldehyde dehydrogenase"
FT /id="PRO_1000140271"
FT ACT_SITE 246
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01275"
FT ACT_SITE 280
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01275"
FT BINDING 146..148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01275"
FT BINDING 172..175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01275"
FT BINDING 209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01275"
FT BINDING 225..228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01275"
FT BINDING 280
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01275"
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
