Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei146NAD; via carbonyl oxygen1 Publication1
Binding sitei209NAD1 Publication1
Active sitei246By similarity1
Active sitei280NucleophileCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi172 – 175NAD1 Publication4
Nucleotide bindingi225 – 231NAD1 Publication7

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
ChainiPRO_00000565631 – 474Gamma-aminobutyraldehyde dehydrogenaseAdd BLAST474

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 interactors.
DIPiDIP-11656N.
IntActiP77674. 4 interactors.
STRINGi511145.b1444.

Structurei

Secondary structure

1474
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 7Combined sources3
Beta strandi10 – 12Combined sources3
Beta strandi18 – 22Combined sources5
Turni24 – 26Combined sources3
Beta strandi29 – 34Combined sources6
Helixi38 – 55Combined sources18
Helixi60 – 76Combined sources17
Helixi78 – 89Combined sources12
Helixi93 – 98Combined sources6
Helixi100 – 114Combined sources15
Beta strandi119 – 121Combined sources3
Beta strandi123 – 127Combined sources5
Beta strandi130 – 138Combined sources9
Beta strandi140 – 145Combined sources6
Beta strandi148 – 150Combined sources3
Helixi151 – 164Combined sources14
Beta strandi168 – 172Combined sources5
Helixi179 – 188Combined sources10
Turni189 – 191Combined sources3
Beta strandi196 – 199Combined sources4
Turni204 – 207Combined sources4
Helixi208 – 212Combined sources5
Beta strandi217 – 224Combined sources8
Helixi226 – 236Combined sources11
Helixi237 – 239Combined sources3
Beta strandi242 – 246Combined sources5
Beta strandi252 – 255Combined sources4
Helixi261 – 271Combined sources11
Helixi274 – 277Combined sources4
Beta strandi285 – 289Combined sources5
Turni290 – 292Combined sources3
Helixi293 – 305Combined sources13
Helixi325 – 340Combined sources16
Beta strandi345 – 348Combined sources4
Beta strandi354 – 357Combined sources4
Beta strandi363 – 366Combined sources4
Helixi373 – 376Combined sources4
Beta strandi381 – 389Combined sources9
Helixi392 – 400Combined sources9
Beta strandi401 – 403Combined sources3
Beta strandi406 – 411Combined sources6
Helixi415 – 424Combined sources10
Beta strandi427 – 433Combined sources7
Helixi448 – 450Combined sources3
Helixi457 – 462Combined sources6
Beta strandi465 – 473Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP77674.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

CDDicd07092. ALDH_ABALDH-YdcW. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WNBX-ray2.20A/B/C/D1-474[»]
1WNDX-ray2.10A/B/C/D1-474[»]
ProteinModelPortaliP77674.
SMRiP77674.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260192. 6 interactors.
DIPiDIP-11656N.
IntActiP77674. 4 interactors.
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

CDDicd07092. ALDH_ABALDH-YdcW. 1 hit.
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: November 2, 2016
This is version 134 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.