Reviewed, UniProtKB/Swiss-Prot Q6D6Y7 (ABDH_ERWCT)

Names and origin

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

Ordered Locus Names:

ECA1542

Organism

Erwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum) [Complete proteome] [HAMAP]

Taxonomic identifier

29471 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the oxidation of 1-pyrroline, which is spontaneously formed from 4-aminobutanal, leading to 4-aminobutanoate (GABA) By similarity.
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.
Miscellaneous	4-aminobutanal is also called gamma-aminobutyraldehyde. HAMAP MF_01275
Sequence similarities	Belongs to the aldehyde dehydrogenase family. Gamma-aminobutyraldehyde dehydrogenase subfamily.

Ontologies

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)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 474	474	Gamma-aminobutyraldehyde dehydrogenase HAMAP MF_01275		PRO_0000269696
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

Sequences

	Sequence		Length	Mass (Da)
	Q6D6Y7-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 675896515A349EE6	FASTA	474	50,838
	10 20 30 40 50 60 MHDKLLIEGK LIAGNGEALA VFNPATGEQI AAIPQADLHQ IDAAVLAAES AFAHWGQTTP 70 80 90 100 110 120 KTRATLLLKI ADAIEENAEV FAKLESLNCG KPYHAVLNDE VPAVADVFRF FAGAARCLSG 130 140 150 160 170 180 SAAGEYLEGH TSMIRRDPVG VVASIAPWNY PLMMASWKLA PALAAGNCVV LKPAEQTPLT 190 200 210 220 230 240 TFYLAHLLAD ILPAGVVNIV FGRGADIGDA LTGHEKVNMV SLTGSIATGA HILAHTAASV 250 260 270 280 290 300 KRTHMELGGK APVIVFDDAD IDQVVDGIRS FGFYNAGQDC TAACRLYVQR AVYDEVVEAL 310 320 330 340 350 360 GKAVATLKIG DPRDETTELG PLITEPQLER VMGFVERAKA LPHITVVTGG ERVKGTGFYF 370 380 390 400 410 420 QPTVLAGAKQ DDEIVQKEVF GPVISITSFD DEAQVIGWAN ASNYGLASSV WTRDIGRAHR 430 440 450 460 470 LAACLQYGCT WVNTHFMLVS EMPHGGQKLS GYGKDMSMYG LEDYTIVRHI MIRH

References

[1]

"Genome sequence of the enterobacterial phytopathogen Erwinia carotovora subsp. atroseptica and characterization of virulence factors." Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z. , Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K. Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004) [PubMed: 15263089] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SCRI 1043 / ATCC BAA-672.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX950851 Genomic DNA. Translation: CAG74448.1.
RefSeq	YP_049644.1.
3D structure databases
SMR	Q6D6Y7. Positions 1-474.
ModBase	Search...
Genome annotation databases
GeneID	2882554.
GenomeReviews	Gene locus ECA1542 in contig BX950851_GR.
KEGG	eca:ECA1542.
NMPDR	fig|218491.3.peg.4057.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6D6Y7.
OMA	QVLRWAN.
Enzyme and pathway databases
BioCyc	ECAR218491:ECA1542-MON.
BRENDA	1.2.1.19. 281579.
Family and domain databases
HAMAP	MF_01275. [Tree]
InterPro	IPR017749. 1-pyrroline_dehydrogenase. 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]
TIGRFAMs	TIGR03374. ABALDH. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. False negative. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ABDH_ERWCT

Accession

Primary (citable) accession number: Q6D6Y7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	August 16, 2004
Last modified:	November 3, 2009
This is version 38 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)