UniProtKB - P25526 (GABD_ECOLI)
Protein
Succinate-semialdehyde dehydrogenase [NADP(+)] GabD
Gene
gabD
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the NADP+-dependent oxidation of succinate semialdehyde to succinate (PubMed:20174634). Thereby functions in a GABA degradation pathway that allows some E.coli strains to utilize GABA as a nitrogen source for growth (PubMed:7011797). Also catalyzes the conversion of glutarate semialdehyde to glutarate, as part of a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate (PubMed:30498244).1 Publication2 Publications
Catalytic activityi
- EC:1.2.1.791 PublicationThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
Kineticsi
The succinate-semialdehyde dehydrogenase activity measured in the presence of NADP+ is approximately 20-fold higher than that measured in the presence of NAD+.
- KM=16.94 µM for succinate semialdehyde1 Publication
: 4-aminobutanoate degradation Pathwayi
This protein is involved in the pathway 4-aminobutanoate degradation, which is part of Amino-acid degradation.1 PublicationView all proteins of this organism that are known to be involved in the pathway 4-aminobutanoate degradation and in Amino-acid degradation.
Pathwayi: Amino-acid degradation
This protein is involved in Amino-acid degradation.1 PublicationView all proteins of this organism that are known to be involved in Amino-acid degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 255 | Proton acceptor1 Publication | 1 | |
Binding sitei | 256 | NADP; via carbonyl oxygen1 Publication | 1 | |
Active sitei | 289 | Nucleophile1 Publication | 1 | |
Binding sitei | 386 | NADP1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 156 – 157 | NADP1 Publication | 2 | |
Nucleotide bindingi | 180 – 183 | NADP1 Publication | 4 | |
Nucleotide bindingi | 233 – 234 | NADP1 Publication | 2 |
GO - Molecular functioni
- glutarate-semialdehyde dehydrogenase (NADP+) activity Source: EcoCyc
- NADP binding Source: UniProtKB
- succinate-semialdehyde dehydrogenase (NAD+) activity Source: UniProtKB
- succinate-semialdehyde dehydrogenase (NADP+) activity Source: EcoCyc
- succinate-semialdehyde dehydrogenase [NAD(P)+] activity Source: UniProtKB
GO - Biological processi
- gamma-aminobutyric acid catabolic process Source: UniProtKB
- nitrogen compound metabolic process Source: UniProtKB
- protein homotetramerization Source: EcoCyc
Keywordsi
Molecular function | Oxidoreductase |
Ligand | NADP |
Enzyme and pathway databases
BioCyci | EcoCyc:SUCCSEMIALDDEHYDROG-MONOMER MetaCyc:SUCCSEMIALDDEHYDROG-MONOMER |
BRENDAi | 1.2.1.79, 2026 |
UniPathwayi | UPA00733 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:gabD Ordered Locus Names:b2661, JW2636 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000056572 | 1 – 482 | Succinate-semialdehyde dehydrogenase [NADP(+)] GabDAdd BLAST | 482 |
Proteomic databases
jPOSTi | P25526 |
PaxDbi | P25526 |
PRIDEi | P25526 |
Expressioni
Inductioni
Interactioni
Subunit structurei
Homotetramer.
1 PublicationProtein-protein interaction databases
BioGRIDi | 4259209, 53 interactors |
DIPi | DIP-9723N |
IntActi | P25526, 3 interactors |
STRINGi | 511145.b2661 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P25526 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the aldehyde dehydrogenase family.Curated
Phylogenomic databases
eggNOGi | COG1012, Bacteria |
HOGENOMi | CLU_005391_5_1_6 |
InParanoidi | P25526 |
PhylomeDBi | P25526 |
Family and domain databases
Gene3Di | 3.40.309.10, 1 hit 3.40.605.10, 1 hit |
InterProi | View protein in InterPro IPR016161, Ald_DH/histidinol_DH IPR016163, Ald_DH_C IPR016160, Ald_DH_CS_CYS IPR029510, Ald_DH_CS_GLU IPR016162, Ald_DH_N IPR015590, Aldehyde_DH_dom IPR010102, Succ_semiAld_DH |
Pfami | View protein in Pfam PF00171, Aldedh, 1 hit |
SUPFAMi | SSF53720, SSF53720, 1 hit |
TIGRFAMsi | TIGR01780, SSADH, 1 hit |
PROSITEi | View protein in PROSITE PS00070, ALDEHYDE_DEHYDR_CYS, 1 hit PS00687, ALDEHYDE_DEHYDR_GLU, 1 hit |
i Sequence
Sequence statusi: Complete.
P25526-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKLNDSNLFR QQALINGEWL DANNGEAIDV TNPANGDKLG SVPKMGADET
60 70 80 90 100
RAAIDAANRA LPAWRALTAK ERATILRNWF NLMMEHQDDL ARLMTLEQGK
110 120 130 140 150
PLAEAKGEIS YAASFIEWFA EEGKRIYGDT IPGHQADKRL IVIKQPIGVT
160 170 180 190 200
AAITPWNFPA AMITRKAGPA LAAGCTMVLK PASQTPFSAL ALAELAIRAG
210 220 230 240 250
VPAGVFNVVT GSAGAVGNEL TSNPLVRKLS FTGSTEIGRQ LMEQCAKDIK
260 270 280 290 300
KVSLELGGNA PFIVFDDADL DKAVEGALAS KFRNAGQTCV CANRLYVQDG
310 320 330 340 350
VYDRFAEKLQ QAVSKLHIGD GLDNGVTIGP LIDEKAVAKV EEHIADALEK
360 370 380 390 400
GARVVCGGKA HERGGNFFQP TILVDVPANA KVSKEETFGP LAPLFRFKDE
410 420 430 440 450
ADVIAQANDT EFGLAAYFYA RDLSRVFRVG EALEYGIVGI NTGIISNEVA
460 470 480
PFGGIKASGL GREGSKYGIE DYLEIKYMCI GL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M88334 Genomic DNA Translation: AAC36831.1 U00096 Genomic DNA Translation: AAC75708.1 AP009048 Genomic DNA Translation: BAA16524.2 |
PIRi | F65045 |
RefSeqi | NP_417147.1, NC_000913.3 WP_000772831.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC75708; AAC75708; b2661 BAA16524; BAA16524; BAA16524 |
GeneIDi | 948060 |
KEGGi | ecj:JW2636 eco:b2661 |
PATRICi | fig|1411691.4.peg.4080 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M88334 Genomic DNA Translation: AAC36831.1 U00096 Genomic DNA Translation: AAC75708.1 AP009048 Genomic DNA Translation: BAA16524.2 |
PIRi | F65045 |
RefSeqi | NP_417147.1, NC_000913.3 WP_000772831.1, NZ_LN832404.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3JZ4 | X-ray | 2.30 | A/B/C/D | 2-482 | [»] | |
SMRi | P25526 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259209, 53 interactors |
DIPi | DIP-9723N |
IntActi | P25526, 3 interactors |
STRINGi | 511145.b2661 |
Proteomic databases
jPOSTi | P25526 |
PaxDbi | P25526 |
PRIDEi | P25526 |
Genome annotation databases
EnsemblBacteriai | AAC75708; AAC75708; b2661 BAA16524; BAA16524; BAA16524 |
GeneIDi | 948060 |
KEGGi | ecj:JW2636 eco:b2661 |
PATRICi | fig|1411691.4.peg.4080 |
Organism-specific databases
EchoBASEi | EB1305 |
Phylogenomic databases
eggNOGi | COG1012, Bacteria |
HOGENOMi | CLU_005391_5_1_6 |
InParanoidi | P25526 |
PhylomeDBi | P25526 |
Enzyme and pathway databases
UniPathwayi | UPA00733 |
BioCyci | EcoCyc:SUCCSEMIALDDEHYDROG-MONOMER MetaCyc:SUCCSEMIALDDEHYDROG-MONOMER |
BRENDAi | 1.2.1.79, 2026 |
Miscellaneous databases
PROi | PR:P25526 |
Family and domain databases
Gene3Di | 3.40.309.10, 1 hit 3.40.605.10, 1 hit |
InterProi | View protein in InterPro IPR016161, Ald_DH/histidinol_DH IPR016163, Ald_DH_C IPR016160, Ald_DH_CS_CYS IPR029510, Ald_DH_CS_GLU IPR016162, Ald_DH_N IPR015590, Aldehyde_DH_dom IPR010102, Succ_semiAld_DH |
Pfami | View protein in Pfam PF00171, Aldedh, 1 hit |
SUPFAMi | SSF53720, SSF53720, 1 hit |
TIGRFAMsi | TIGR01780, SSADH, 1 hit |
PROSITEi | View protein in PROSITE PS00070, ALDEHYDE_DEHYDR_CYS, 1 hit PS00687, ALDEHYDE_DEHYDR_GLU, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GABD_ECOLI | |
Accessioni | P25526Primary (citable) accession number: P25526 Secondary accession number(s): P78207, P78208, P78209 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 1992 |
Last sequence update: | May 1, 1992 | |
Last modified: | April 7, 2021 | |
This is version 164 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families