ABDH_SALTY
ID ABDH_SALTY Reviewed; 474 AA.
AC Q8ZPC9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
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=STM1597;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAL20515.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006468; AAL20515.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_460556.3; NC_003197.2.
DR PDB; 6C43; X-ray; 2.90 A; A/B/C/D/E/F/G/H=1-474.
DR PDBsum; 6C43; -.
DR AlphaFoldDB; Q8ZPC9; -.
DR SMR; Q8ZPC9; -.
DR STRING; 99287.STM1597; -.
DR PaxDb; Q8ZPC9; -.
DR EnsemblBacteria; AAL20515; AAL20515; STM1597.
DR GeneID; 1253115; -.
DR KEGG; stm:STM1597; -.
DR PATRIC; fig|99287.12.peg.1688; -.
DR HOGENOM; CLU_005391_0_2_6; -.
DR OMA; NDDLGEV; -.
DR PhylomeDB; Q8ZPC9; -.
DR UniPathway; UPA00188; UER00292.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..474
FT /note="Gamma-aminobutyraldehyde dehydrogenase"
FT /id="PRO_0000269700"
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"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:6C43"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 38..55
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 60..76
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:6C43"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:6C43"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:6C43"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:6C43"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 325..340
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 381..389
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 392..400
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 415..424
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:6C43"
FT HELIX 457..462
FT /evidence="ECO:0007829|PDB:6C43"
FT STRAND 465..473
FT /evidence="ECO:0007829|PDB:6C43"
SQ SEQUENCE 474 AA; 51191 MW; 69A772AC65753601 CRC64;
MQYQLLINGV LVDGEGERQS VYNPATGEVI LEIAEASPAQ VDAAVQAADN AFAEWGQTTP
KARAECLLKL ADSIEQNALE FARLESQNCG KPLHCVINDE IPAIVDVFRF FAGAARCLSG
LAAGEYLEGH TSMIRRDPIG VVASIAPWNY PLMMAAWKLA PALAAGNCVV IKPSEITPLT
ALKLAVLAKD IFPPGVLNVL FGRGQTVGDV LTGHEKVRMV SLTGSIATGE HILRHTAPAI
KRTHMELGGK APVIVFDDAD LDAVAQGVRT FGFYNAGQDC TAACRIYAQR GIYDALVEKL
GNAVSSLKMG APEDESTELG PLSSLAHLKR VTAAVEEAKA LSHIRVITGG SQTEGKGYYF
APTLLADAKQ EDAIVQREVF GPVVSITVFD DEDQVLRWAN DSRYGLASSV WTQDVGRAHR
LSARLQYGCT WINTHFMLVS EMPHGGQKQS GYGKDMSLYG LEDYTLVRHI MVKH
