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Protein

Gamma-aminobutyraldehyde dehydrogenase

Gene

prr

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH.

Kineticsi

  1. KM=41 µM for 4-aminobutanal1 Publication
  2. KM=196 µM for butanal1 Publication
  3. KM=54 µM for NAD+1 Publication
  4. KM=484 µM for NADP+1 Publication
  1. Vmax=9.08 µmol/min/mg enzyme with 4-aminobutanal as substrate1 Publication
  2. Vmax=0.36 µmol/min/mg enzyme with butanal as substrate1 Publication

Pathwayi: putrescine degradation

This protein is involved in step 1 of the subpathway that synthesizes 4-aminobutanoate from 4-aminobutanal.
Proteins known to be involved in this subpathway in this organism are:
  1. Gamma-aminobutyraldehyde dehydrogenase (prr)
This subpathway is part of the pathway putrescine degradation, which is itself part of Amine and polyamine degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 4-aminobutanoate from 4-aminobutanal, the pathway putrescine degradation and in Amine and polyamine degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei146 – 1461NAD; via carbonyl oxygen1 Publication
Binding sitei209 – 2091NAD1 Publication
Active sitei246 – 2461By similarity
Active sitei280 – 2801NucleophileCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi172 – 1754NAD1 Publication
Nucleotide bindingi225 – 2317NAD1 Publication

GO - Molecular functioni

  • 1-pyrroline dehydrogenase activity Source: EcoCyc
  • aminobutyraldehyde dehydrogenase activity Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • NAD binding Source: UniProtKB-HAMAP

GO - Biological processi

  • putrescine catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciEcoCyc:G6755-MONOMER.
ECOL316407:JW1439-MONOMER.
MetaCyc:G6755-MONOMER.
BRENDAi1.2.1.19. 2026.
SABIO-RKP77674.
UniPathwayiUPA00188; UER00292.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-aminobutyraldehyde dehydrogenase (EC:1.2.1.19)
Alternative name(s):
1-pyrroline dehydrogenase
4-aminobutanal dehydrogenase
Short name:
ABALDH
Gene namesi
Name:prr
Synonyms:ydcW
Ordered Locus Names:b1444, JW1439
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13766. prr.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 474474Gamma-aminobutyraldehyde dehydrogenasePRO_0000056563Add
BLAST

Proteomic databases

EPDiP77674.
PaxDbiP77674.
PRIDEiP77674.

Expressioni

Inductioni

Up-regulated under nitrogen starvation conditions.1 Publication

Interactioni

Subunit structurei

Homotetramer.2 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260192. 6 interactions.
DIPiDIP-11656N.
IntActiP77674. 4 interactions.
STRINGi511145.b1444.

Structurei

Secondary structure

1
474
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Beta strandi10 – 123Combined sources
Beta strandi18 – 225Combined sources
Turni24 – 263Combined sources
Beta strandi29 – 346Combined sources
Helixi38 – 5518Combined sources
Helixi60 – 7617Combined sources
Helixi78 – 8912Combined sources
Helixi93 – 986Combined sources
Helixi100 – 11415Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi123 – 1275Combined sources
Beta strandi130 – 1389Combined sources
Beta strandi140 – 1456Combined sources
Beta strandi148 – 1503Combined sources
Helixi151 – 16414Combined sources
Beta strandi168 – 1725Combined sources
Helixi179 – 18810Combined sources
Turni189 – 1913Combined sources
Beta strandi196 – 1994Combined sources
Turni204 – 2074Combined sources
Helixi208 – 2125Combined sources
Beta strandi217 – 2248Combined sources
Helixi226 – 23611Combined sources
Helixi237 – 2393Combined sources
Beta strandi242 – 2465Combined sources
Beta strandi252 – 2554Combined sources
Helixi261 – 27111Combined sources
Helixi274 – 2774Combined sources
Beta strandi285 – 2895Combined sources
Turni290 – 2923Combined sources
Helixi293 – 30513Combined sources
Helixi325 – 34016Combined sources
Beta strandi345 – 3484Combined sources
Beta strandi354 – 3574Combined sources
Beta strandi363 – 3664Combined sources
Helixi373 – 3764Combined sources
Beta strandi381 – 3899Combined sources
Helixi392 – 4009Combined sources
Beta strandi401 – 4033Combined sources
Beta strandi406 – 4116Combined sources
Helixi415 – 42410Combined sources
Beta strandi427 – 4337Combined sources
Helixi448 – 4503Combined sources
Helixi457 – 4626Combined sources
Beta strandi465 – 4739Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WNBX-ray2.20A/B/C/D1-474[»]
1WNDX-ray2.10A/B/C/D1-474[»]
ProteinModelPortaliP77674.
SMRiP77674. Positions 1-474.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77674.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271505.
InParanoidiP77674.
KOiK00137.
OMAiIRSFGFY.
PhylomeDBiP77674.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPiMF_01275. Aldedh_Prr. 1 hit.
InterProiIPR017749. 1-pyrroline_dehydrogenase.
IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR015657. Aminobutyraldehyde_DH.
[Graphical view]
PANTHERiPTHR11699:SF109. PTHR11699:SF109. 1 hit.
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR03374. ABALDH. 1 hit.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P77674-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQHKLLINGE LVSGEGEKQP VYNPATGDVL LEIAEASAEQ VDAAVRAADA
60 70 80 90 100
AFAEWGQTTP KVRAECLLKL ADVIEENGQV FAELESRNCG KPLHSAFNDE
110 120 130 140 150
IPAIVDVFRF FAGAARCLNG LAAGEYLEGH TSMIRRDPLG VVASIAPWNY
160 170 180 190 200
PLMMAAWKLA PALAAGNCVV LKPSEITPLT ALKLAELAKD IFPAGVINIL
210 220 230 240 250
FGRGKTVGDP LTGHPKVRMV SLTGSIATGE HIISHTASSI KRTHMELGGK
260 270 280 290 300
APVIVFDDAD IEAVVEGVRT FGYYNAGQDC TAACRIYAQK GIYDTLVEKL
310 320 330 340 350
GAAVATLKSG APDDESTELG PLSSLAHLER VGKAVEEAKA TGHIKVITGG
360 370 380 390 400
EKRKGNGYYY APTLLAGALQ DDAIVQKEVF GPVVSVTPFD NEEQVVNWAN
410 420 430 440 450
DSQYGLASSV WTKDVGRAHR VSARLQYGCT WVNTHFMLVS EMPHGGQKLS
460 470
GYGKDMSLYG LEDYTVVRHV MVKH
Length:474
Mass (Da):50,830
Last modified:February 1, 1997 - v1
Checksum:i487C6044719A41E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74526.1.
AP009048 Genomic DNA. Translation: BAA15073.1.
PIRiG64896.
RefSeqiNP_415961.1. NC_000913.3.
WP_001163872.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74526; AAC74526; b1444.
BAA15073; BAA15073; BAA15073.
GeneIDi945876.
KEGGiecj:JW1439.
eco:b1444.
PATRICi32118178. VBIEscCol129921_1509.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74526.1.
AP009048 Genomic DNA. Translation: BAA15073.1.
PIRiG64896.
RefSeqiNP_415961.1. NC_000913.3.
WP_001163872.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WNBX-ray2.20A/B/C/D1-474[»]
1WNDX-ray2.10A/B/C/D1-474[»]
ProteinModelPortaliP77674.
SMRiP77674. Positions 1-474.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260192. 6 interactions.
DIPiDIP-11656N.
IntActiP77674. 4 interactions.
STRINGi511145.b1444.

Proteomic databases

EPDiP77674.
PaxDbiP77674.
PRIDEiP77674.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74526; AAC74526; b1444.
BAA15073; BAA15073; BAA15073.
GeneIDi945876.
KEGGiecj:JW1439.
eco:b1444.
PATRICi32118178. VBIEscCol129921_1509.

Organism-specific databases

EchoBASEiEB3529.
EcoGeneiEG13766. prr.

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271505.
InParanoidiP77674.
KOiK00137.
OMAiIRSFGFY.
PhylomeDBiP77674.

Enzyme and pathway databases

UniPathwayiUPA00188; UER00292.
BioCyciEcoCyc:G6755-MONOMER.
ECOL316407:JW1439-MONOMER.
MetaCyc:G6755-MONOMER.
BRENDAi1.2.1.19. 2026.
SABIO-RKP77674.

Miscellaneous databases

EvolutionaryTraceiP77674.
PROiP77674.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPiMF_01275. Aldedh_Prr. 1 hit.
InterProiIPR017749. 1-pyrroline_dehydrogenase.
IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR015657. Aminobutyraldehyde_DH.
[Graphical view]
PANTHERiPTHR11699:SF109. PTHR11699:SF109. 1 hit.
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR03374. ABALDH. 1 hit.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiABDH_ECOLI
AccessioniPrimary (citable) accession number: P77674
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: September 7, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

4-aminobutanal is also called gamma-aminobutyraldehyde.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.