ABDH_SERP5
ID ABDH_SERP5 Reviewed; 474 AA.
AC A8GHZ8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Spro_3642;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-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; CP000826; ABV42738.1; -; Genomic_DNA.
DR RefSeq; WP_012146349.1; NC_009832.1.
DR AlphaFoldDB; A8GHZ8; -.
DR SMR; A8GHZ8; -.
DR STRING; 399741.Spro_3642; -.
DR EnsemblBacteria; ABV42738; ABV42738; Spro_3642.
DR KEGG; spe:Spro_3642; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_6; -.
DR OMA; IRAFGFY; -.
DR OrthoDB; 744602at2; -.
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_1000067395"
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; 50984 MW; E028C995EBC8A3FD CRC64;
MQSQLLINGQ LVTGQGALLP VYNPATGEVV VQVAEASAEQ VDQAVLAADA AFEHWGQTTP
KERAEHLLKL ADLIDSHAET FARLESINCG KPYHCVLNDE LPGVADVFRF FAGASRCLSG
LAAGEYLAGH TSMIRRDPLG VVASIAPWNY PLMMAAWKLA PALAAGNCVV LKPSEQTPLT
TFKLAELAAG LFPPGVLNVL FGRGASVGDR LTGHNKVRMV SLTGSIATGE HIIGHTASGI
KRTHMELGGK APVLVFDDAD LQQVVEGIRS FGFYNAGQDC TAACRIYAQK GIYPQLVKAL
GEAIGSLKIG PPIDASSELG PLITAQHLER VVGFVERAKA LPHVQVVTGG ERVNGPGYYF
QPTLLAGARQ EDEIVQREVF GPVVTVTPFD DEAQVLAWAN ESDYGLASSL WTRDVGRAHR
LSARLQYGCT WVNTHFMLVS EMPHGGQKLS GYGKDMSMYG LEDYTAIRHV MFKH
