A8AGJ9 (ABDH_CITK8) 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:	CKO_01478

Organism

Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) [Complete proteome] [HAMAP]

Taxonomic identifier

290338 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Citrobacter

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	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_1000067390
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)
	A8AGJ9 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: F9C378301CB80BF1	FASTA	474	50,950
	10 20 30 40 50 60 MPHQLLINGE LVSGEGEKQP VYNPATGEVI LEIAEASPAQ VDAAVRAADR AFAEWGQTTP 70 80 90 100 110 120 KARAELLLTL ADVIEENAQT FAELESQNCG KPLHCALNDE IPAIVDVFRF FAGAARCLNG 130 140 150 160 170 180 LAAGEYLEGH TSMIRRDPVG VVASIAPWNY PLMMAAWKLA PALAAGNCVV IKPSEITPLT 190 200 210 220 230 240 ALKLAEFAKD IFPPGVLNVL FGRGKTVGDP LTGHEKVRMV SLTGSIATGE HIIQHTAPSI 250 260 270 280 290 300 KRTHMELGGK APVIVFDDAD LDAVVEGVRT FGFYNAGQDC TAACRIYAQK GIYDALVEKL 310 320 330 340 350 360 GAAVASLKTG SPNDESTELG PLSSQAHLER VTKAVEEAKA LGHINVVTGG QKLDGAGYYF 370 380 390 400 410 420 APTLLAGAKQ EDAIVQREVF GPVVSMTVFD DEEQVLAWAN DTQYGLASSV WTKDVGRAHR 430 440 450 460 470 LSARLQYGCT WVNTHFMLVS EMPHGGQKRS GYGKDMSLYG LEDYTVIRHI MVKH

References

[1]

The Citrobacter koseri Genome Sequencing Project McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R. Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-895 / CDC 4225-83 / SGSC4696.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000822 Genomic DNA. Translation: ABV12611.1.
RefSeq	YP_001453048.1. NC_009792.1.
3D structure databases
ProteinModelPortal	A8AGJ9.
SMR	A8AGJ9. Positions 1-474.
ModBase	Search...
Protein-protein interaction databases
STRING	A8AGJ9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5581967.
GenomeReviews	Gene locus CKO_01478 in contig CP000822_GR.
KEGG	cko:CKO_01478.
PATRIC	20386053. VBICitKos71230_1244.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1012.
HOGENOM	HBG752218.
OMA	QVLRWAN.
ProtClustDB	PRK13473.
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_CITK8

Accession

Primary (citable) accession number: A8AGJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	January 25, 2012
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program