Reviewed, UniProtKB/Swiss-Prot Q0T431 (ABDH_SHIF8)

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

Name:	ydcW
Ordered Locus Names:	SFV_1770

Organism

Shigella flexneri serotype 5b (strain 8401) [Complete proteome] [HAMAP]

Taxonomic identifier

373384 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
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. 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.

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_1000067396
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)
	Q0T431-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: B07699F3CB34713F	FASTA	474	50,860
	10 20 30 40 50 60 MQHKLLINGE LVSGEGEKQP VYNPATGDVL LEIAEVSAEQ VDAAVRAADA AFAEWGQTTP 70 80 90 100 110 120 KARAECLLKL ADVIEENGQV FAELESRNCG KPLHSAFNDE IPAIVDVFRF FAGAARCLNG 130 140 150 160 170 180 LAAGEYLEGH TSMIRRDPLG VVASIAPWNY PLMMAAWKLA PALAAGNCVV LKPSEITPLT 190 200 210 220 230 240 ALKLAELAKD IFPAGVINIL FGRGKTVGDP LTGHPKVRMV SLTGSIATGE HIISHTASSI 250 260 270 280 290 300 KRTHMELGGK APVIVFDDAD IEAVVEGVRT FGYYNAGQDC TAACRIYAQK GIYDTLVEKL 310 320 330 340 350 360 GAAVATLKSG APDDESTELG PLSSLAHLER VSKAVEEAKA TGHIKVITGG EKRKGNGYYY 370 380 390 400 410 420 APTLLAGALQ DDAIVQKEVF GPVVSVTPFD NEEQVVNWAN DSQYGLASSV WTKDVGRAHR 430 440 450 460 470 VSARLQYGCT WVNTHFMLVS EMPHGGQKLS GYGKDMSLYG LEDYTVVRHV MVKH

References

[1]

"Complete genome sequence of Shigella flexneri 5b and comparison with Shigella flexneri 2a." Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q. BMC Genomics 7:173-173(2006) [PubMed: 16822325] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000266 Genomic DNA. Translation: ABF03934.1.
RefSeq	YP_689239.1.
3D structure databases
SMR	Q0T431. Positions 1-474.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0T431.
Genome annotation databases
GeneID	4208338.
GenomeReviews	Gene locus SFV_1770 in contig CP000266_GR.
KEGG	sfv:SFV_1770.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1012.
HOGENOM	HBG752218.
OMA	GYYFQPT.
Enzyme and pathway databases
BioCyc	SFLE373384:SFV_1770-MONOMER.
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]
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_SHIF8

Accession

Primary (citable) accession number: Q0T431

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 5, 2006
Last modified:	February 9, 2010
This is version 31 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)