Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Gamma-aminobutyraldehyde dehydrogenase |
Protein Synonyms/Alias | ABALDH |
Gene Name | prr |
Gene Synonyms/Alias | ydcW; OrderedLocusNames=b1444, JW1439 |
Created Date | 3-June-2014 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Phosphorylation | Position | Peptide | Code | Type | References | 13 | LINGELVSGEGEKQP | S | HTP | [1] | |
Reference | [1]Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium. Soares NC,Spät P,Krug K,Macek B J. Proteome Res. 2013, Jun, 7;12(6):2611-21. [ PMID:23590516] |
Functional Description From UniProt | 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 |
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| 3D-structure; Completeproteome; NAD; Oxidoreductase; Referenceproteome |
Protein Sequence | MQHKLLINGE LVSGEGEKQP VYNPATGDVL LEIAEASAEQ VDAAVRAADA AFAEWGQTTP 60 KVRAECLLKL ADVIEENGQV FAELESRNCG KPLHSAFNDE IPAIVDVFRF FAGAARCLNG 120 LAAGEYLEGH TSMIRRDPLG VVASIAPWNY PLMMAAWKLA PALAAGNCVV LKPSEITPLT 180 ALKLAELAKD IFPAGVINIL FGRGKTVGDP LTGHPKVRMV SLTGSIATGE HIISHTASSI 240 KRTHMELGGK APVIVFDDAD IEAVVEGVRT FGYYNAGQDC TAACRIYAQK GIYDTLVEKL 300 GAAVATLKSG APDDESTELG PLSSLAHLER VGKAVEEAKA TGHIKVITGG EKRKGNGYYY 360 APTLLAGALQ DDAIVQKEVF GPVVSVTPFD NEEQVVNWAN DSQYGLASSV WTKDVGRAHR 420 VSARLQYGCT WVNTHFMLVS EMPHGGQKLS GYGKDMSLYG LEDYTVVRHV MVKH 474 |
| GO:0033737 F:1-pyrroline dehydrogenase activity IMP:EcoCyc GO:0019145 F:aminobutyraldehyde dehydrogenase activity IDA:EcoCyc GO:0042802 F:identical protein binding IDA:EcoCyc GO:0051287 F:NAD binding IEA:UniProtKB-HAMAP GO:0009447 P:putrescine catabolic process IMP:EcoCyc |
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