Q5PHV8 (ABDH_SALPA) Reviewed, UniProtKB/Swiss-Prot

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:	prr
Ordered Locus Names:	SPA1271

Organism

Salmonella paratyphi A [Complete proteome] [HAMAP]

Taxonomic identifier

54388 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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.
Sequence caution	The sequence AAV77220.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	putrescine catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	1-pyrroline dehydrogenase activity Inferred from electronic annotation. Source: EC NAD binding Inferred from electronic annotation. Source: InterPro aminobutyraldehyde dehydrogenase activity Inferred from electronic annotation. Source: EC
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_0000269698
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)
	Q5PHV8 [UniParc]. Last modified January 9, 2007. Version 2. Checksum: 46373A0205DC51AC	FASTA	474	51,178
	10 20 30 40 50 60 MQYQLLINGV LVDGEGERQS VYNPATGEVI LEIAEASPAQ IDAAVQAAVN TFAEWGQTTP 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 APEDESTELG PLSSLAHLKR VTAAVEEAKA LSHIRVITGG SQTEGKGYYF 370 380 390 400 410 420 APTLLADAKQ EDAIVQREVF GPVVSITVFD DEDQVLRWGN DSRYGLASSV WTQDVGRAHR 430 440 450 460 470 LSARLQYGCT WINTHFMLVS EMPHGGQKQS GYGKDMSLYG LEDYTLVRHI MVKH

References

[1]

"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid." McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K. Nat. Genet. 36:1268-1274(2004) [PubMed: 15531882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000026 Genomic DNA. Translation: AAV77220.1. Different initiation.
RefSeq	YP_150532.2. NC_006511.1.
3D structure databases
HSSP	HSSP built from PDB template 1WND based on UniProtKB P77674.
ProteinModelPortal	Q5PHV8.
SMR	Q5PHV8. Positions 1-474.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3177951.
GenomeReviews	Gene locus SPA1271 in contig CP000026_GR.
KEGG	spt:SPA1271.
NMPDR	fig|295319.3.peg.2456.
PATRIC	32351843. VBISalEnt134188_1355.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG752218.
OMA	QVLRWAN.
ProtClustDB	PRK13473.
Enzyme and pathway databases
BioCyc	SENT295319:SPA1271-MONOMER.
Family and domain databases
HAMAP	MF_01275. Aldedh_Prr. [Tree]
InterPro	IPR017749. 1-pyrroline_dehydrogenase. IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. [Graphical view]
Gene3D	G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
KO	K00137.
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 information

Entry name

ABDH_SALPA

Accession

Primary (citable) accession number: Q5PHV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	January 9, 2007
Last modified:	January 25, 2012
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program