Reviewed, UniProtKB/Swiss-Prot A9MYQ4 (ABDH_SALPB)

Names and originHide

Protein names

Recommended name:
Gamma-aminobutyraldehyde dehydrogenase
EC=1.2.1.19

Alternative name(s):
1-pyrroline dehydrogenase
4-aminobutanal dehydrogenase
Short name=ABALDH

Gene names

Name:	ydcW
Ordered Locus Names:	SPAB_01688

Organism

Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) [Complete proteome] [HAMAP]

Taxonomic identifier

272994 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella enterica subsp. enterica serovar Paratyphi B

Protein attributesHide

Sequence length	474 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)Hide

Function	Catalyzes the oxidation of 1-pyrroline, which is spontaneously formed from 4-aminobutanal, leading to 4-aminobutanoate (GABA) By similarity. HAMAP MF_01275
Catalytic activity	4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH. HAMAP MF_01275
Pathway	Amine and polyamine degradation; putrescine degradation; 4-aminobutanoate from 4-aminobutanal: step 1/1. HAMAP MF_01275
Subunit structure	Homotetramer By similarity. HAMAP MF_01275
Miscellaneous	4-aminobutanal is also called gamma-aminobutyraldehyde. HAMAP MF_01275
Sequence similarities	Belongs to the aldehyde dehydrogenase family. Gamma-aminobutyraldehyde dehydrogenase subfamily.

OntologiesHide

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW putrescine catabolic process Inferred from electronic annotation. Source: HAMAP
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: HAMAP aminobutyraldehyde dehydrogenase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)Hide

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 474	474	Gamma-aminobutyraldehyde dehydrogenase HAMAP MF_01275		PRO_1000085863
Regions
	Nucleotide binding	172 – 175	4	NAD By similarity
	Nucleotide binding	225 – 231	7	NAD By similarity
Sites
	Active site	246	1	By similarity
	Active site	280	1	Nucleophile By similarity
	Binding site	146	1	NAD; via carbonyl oxygen By similarity
	Binding site	209	1	NAD By similarity

SequencesHide

	Sequence		Length	Mass (Da)
	A9MYQ4-1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 345301254B66972F	FASTA	474	51,179
	10 20 30 40 50 60 MQYQLLINGV LVDGEGERQS VYNPATGEVI LEIAEASPAQ VDAAVLAADS AFAEWGQTTP 70 80 90 100 110 120 KARAECLLKL ADSIEQNALE FARLESQNCG KPLHCVINDE IPAIVDVFRF FAGAARCLSG 130 140 150 160 170 180 LAAGEYLEGH TSMIRRDPIG VVASIAPWNY PLMMAAWKLA PALAAGNCVV IKPSEITPLT 190 200 210 220 230 240 ALKLAALAKD IFPPGVLNVL FGRGQTVGDV LTGHEKVRMV SLTGSIATGE HILRHTAPAI 250 260 270 280 290 300 KRTHMELGGK APVIVFDDAD LDAVAQGVRT FGFYNAGQDC TAACRIYAQR GIYDALVEKL 310 320 330 340 350 360 GNAVSSLKMG TPEDESTELG PLSSLAHLKR VTAAVEEAKA LSHIRVITGG SQTEGKGYYF 370 380 390 400 410 420 APTLLADARQ EDAIVQREVF GPVVSITVFD DEDQVLRWAN DSRYGLASSV WTQDVGRAHR 430 440 450 460 470 LSARLQYGCT WINTHFMLVS EMPHGGQKQS GYGKDMSLYG LEDYTLVRHI MVKH

ReferencesHide

[1]	McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-referencesHide

Sequence databases
EMBL GenBank DDBJ	CP000886 Genomic DNA. Translation: ABX67082.1.
RefSeq	YP_001587915.1.
3D structure databases
SMR	A9MYQ4. Positions 1-474.
ModBase	Search...
Genome annotation databases
GeneID	5783567.
GenomeReviews	Gene locus SPAB_01688 in contig CP000886_GR.
KEGG	spq:SPAB_01688.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG752218.
OMA	QVLRWAN.
ProtClustDB	PRK13473.
Family and domain databases
HAMAP	MF_01275. Aldedh_YdcW. [Tree]
InterPro	IPR017749. 1-pyrroline_dehydrogenase. IPR016161. Ald_DH/histidinol_DH. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMs	TIGR03374. ABALDH. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. False negative. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...

Entry informationHide

Entry name

ABDH_SALPB

Accession

Primary (citable) accession number: A9MYQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	March 2, 2010
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)