Reviewed, UniProtKB/Swiss-Prot P77674 (ABDH_ECOLI)

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:	b1444, JW1439

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the oxidation of 1-pyrroline, which is spontaneously formed from 4-aminobutanal, leading to 4-aminobutanoate (GABA). Can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency. Ref.4 Ref.5
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. Ref.4 Ref.5
Induction	Up-regulated under nitrogen starvation conditions. Ref.4
Miscellaneous	4-aminobutanal is also called gamma-aminobutyraldehyde. HAMAP MF_01275
Sequence similarities	Belongs to the aldehyde dehydrogenase family. Gamma-aminobutyraldehyde dehydrogenase subfamily.
Biophysicochemical properties	Kinetic parameters: KM=41 µM for 4-aminobutanal Ref.4 KM=196 µM for butanal KM=54 µM for NAD+ KM=484 µM for NADP+ Vmax=9.08 µmol/min/mg enzyme with 4-aminobutanal as substrate Vmax=0.36 µmol/min/mg enzyme with butanal as substrate

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure 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_0000056563

Regions

Nucleotide binding

172 – 175

4

NAD HAMAP MF_01275

Nucleotide binding

225 – 231

7

NAD HAMAP MF_01275

Sites

Active site

246

1

By similarity

Active site

280

1

Nucleophile Probable

Binding site

146

1

NAD; via carbonyl oxygen HAMAP MF_01275

Binding site

209

1

NAD HAMAP MF_01275

Secondary structure

1

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474

Helix Strand Turn

Details...

Beta strand

5 – 7

3

Beta strand

10 – 12

3

Beta strand

18 – 22

5

Turn

24 – 26

3

Beta strand

29 – 34

6

Helix

38 – 55

18

Helix

60 – 76

17

Helix

78 – 89

12

Helix

93 – 98

6

Helix

100 – 114

15

Beta strand

119 – 121

3

Beta strand

123 – 127

5

Beta strand

130 – 138

9

Beta strand

140 – 145

6

Beta strand

148 – 150

3

Helix

151 – 164

14

Beta strand

168 – 172

5

Helix

179 – 188

10

Turn

189 – 191

3

Beta strand

196 – 199

4

Turn

204 – 207

4

Helix

208 – 212

5

Beta strand

217 – 224

8

Helix

226 – 235

10

Helix

237 – 239

3

Beta strand

242 – 246

5

Beta strand

252 – 255

4

Helix

261 – 271

11

Helix

274 – 277

4

Beta strand

285 – 289

5

Turn

290 – 292

3

Helix

293 – 304

12

Helix

325 – 339

15

Beta strand

345 – 348

4

Beta strand

354 – 357

4

Beta strand

363 – 367

5

Helix

373 – 376

4

Beta strand

381 – 389

9

Helix

392 – 400

9

Beta strand

401 – 403

3

Beta strand

406 – 411

6

Helix

415 – 424

10

Beta strand

427 – 433

7

Helix

448 – 450

3

Helix

457 – 462

6

Beta strand

465 – 473

9

Sequences

	Sequence		Length	Mass (Da)
	P77674-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 487C6044719A41E3	FASTA	474	50,830
	10 20 30 40 50 60 MQHKLLINGE LVSGEGEKQP VYNPATGDVL LEIAEASAEQ VDAAVRAADA AFAEWGQTTP 70 80 90 100 110 120 KVRAECLLKL 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 VGKAVEEAKA 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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Identification of Escherichia coli K12 YdcW protein as a gamma-aminobutyraldehyde dehydrogenase." Samsonova N.N., Smirnov S.V., Novikova A.E., Ptitsyn L.R. FEBS Lett. 579:4107-4112(2005) [PubMed: 16023116] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, INDUCTION, KINETIC PARAMETERS. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase." Gruez A., Roig-Zamboni V., Grisel S., Salomoni A., Valencia C., Campanacci V., Tegoni M., Cambillau C. J. Mol. Biol. 343:29-41(2004) [PubMed: 15381418] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, FUNCTION, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U00096 Genomic DNA. Translation: AAC74526.1.
AP009048 Genomic DNA. Translation: BAA15073.1.

PIR

G64896.

RefSeq

AP_002067.1.
NP_415961.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WNB	X-ray	2.20	A/B/C/D	1-474	[»]
1WND	X-ray	2.10	A/B/C/D	1-474	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P77674.

Proteomic databases

PRIDE

P77674.

Genome annotation databases

GeneID

945876.

GenomeReviews

Gene locus JW1439 in contig AP009048_GR.
Gene locus b1444 in contig U00096_GR.

KEGG

ecj:JW1439.
eco:b1444.

Organism-specific databases

EchoBASE

EB3529.

EcoGene

EG13766. ydcW.

CMR

Search...

Phylogenomic databases

HOGENOM

P77674.

OMA

GYYFQPT.

Enzyme and pathway databases

BioCyc

EcoCyc:G6755-MON.
MetaCyc:G6755-MON.

BRENDA

1.2.1.19. 246.

Gene expression databases

Genevestigator

P77674.

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_ECOLI

Accession

Primary (citable) accession number: P77674

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 1, 1997
Last modified:	November 3, 2009
This is version 78 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)