ABDH_CITK8
ID ABDH_CITK8 Reviewed; 474 AA.
AC A8AGJ9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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}; OrderedLocusNames=CKO_01478;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000822; ABV12611.1; -; Genomic_DNA.
DR RefSeq; WP_012132353.1; NC_009792.1.
DR AlphaFoldDB; A8AGJ9; -.
DR SMR; A8AGJ9; -.
DR STRING; 290338.CKO_01478; -.
DR EnsemblBacteria; ABV12611; ABV12611; CKO_01478.
DR GeneID; 45135552; -.
DR KEGG; cko:CKO_01478; -.
DR HOGENOM; CLU_005391_0_0_6; -.
DR OMA; NDDLGEV; -.
DR OrthoDB; 744602at2; -.
DR UniPathway; UPA00188; UER00292.
DR Proteomes; UP000008148; Chromosome.
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; Reference proteome.
FT CHAIN 1..474
FT /note="Gamma-aminobutyraldehyde dehydrogenase"
FT /id="PRO_1000067390"
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; 50950 MW; F9C378301CB80BF1 CRC64;
MPHQLLINGE LVSGEGEKQP VYNPATGEVI LEIAEASPAQ VDAAVRAADR AFAEWGQTTP
KARAELLLTL ADVIEENAQT FAELESQNCG KPLHCALNDE IPAIVDVFRF FAGAARCLNG
LAAGEYLEGH TSMIRRDPVG VVASIAPWNY PLMMAAWKLA PALAAGNCVV IKPSEITPLT
ALKLAEFAKD IFPPGVLNVL FGRGKTVGDP LTGHEKVRMV SLTGSIATGE HIIQHTAPSI
KRTHMELGGK APVIVFDDAD LDAVVEGVRT FGFYNAGQDC TAACRIYAQK GIYDALVEKL
GAAVASLKTG SPNDESTELG PLSSQAHLER VTKAVEEAKA LGHINVVTGG QKLDGAGYYF
APTLLAGAKQ EDAIVQREVF GPVVSMTVFD DEEQVLAWAN DTQYGLASSV WTKDVGRAHR
LSARLQYGCT WVNTHFMLVS EMPHGGQKRS GYGKDMSLYG LEDYTVIRHI MVKH
