Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Aldehyde-alcohol dehydrogenase |
Protein Synonyms/Alias | ADH; ACDH; PFL deactivase |
Gene Name | adhE |
Gene Synonyms/Alias | Z2016, ECs1741 |
Created Date | 3-June-2014 |
Organism | Escherichia coli O157:H7 |
NCBI Taxa ID | 83334 |
Phosphorylation | Position | Peptide | Code | Type | References | 766 | KQTAFSQYDRPQARR | Y | HTP | [1] | 75 | KNHFASEYIYNAYKD | Y | HTP | [1] | 384 | NQPARVSYFGQKMKT | Y | HTP | [1] | 80 | SEYIYNAYKDEKTCG | Y | HTP | [1] | 302 | AIVGQPAYKIAELAG | Y | HTP | [1] | 203 | PGMVKAAYSSGKPAI | Y | HTP | [1] | 581 | MDIRKRIYKFPKMGV | Y | HTP | [1] | 690 | KEYLPASYHEGSKNP | Y | HTP | [1] | 77 | HFASEYIYNAYKDEK | Y | HTP | [1] | 409 | QGGIGDLYNFKLAPS | Y | HTP | [1] | 272 | RFATHGGYLLQGKEL | Y | HTP | [1] | 372 | IGHTSCLYTDQDNQP | Y | HTP | [1] | |
Reference | [1]The Escherichia coli phosphotyrosine proteome relates to core pathways and virulence. Hansen AM,Chaerkady R,Sharma J,Díaz-Mejía JJ,Tyagi N,Renuse S,Jacob HK,Pinto SM,Sahasrabuddhe NA,Kim MS,Delanghe B,Srinivasan N,Emili A,Kaper JB,Pandey A PLoS Pathog. 2013;9(6):e1003403. [ PMID:23785281] |
Functional Description From UniProt | FUNCTION: This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction (By similarity) |
| MOD_RES 358 358 N6-acetyllysine (By similarity) |
| Acetylation; Completeproteome; Iron; Multifunctionalenzyme; NAD; Oxidoreductase |
Protein Sequence | MAVTNVAELN ALVERVKKAQ REYASFTQEQ VDKIFRAAAL AAADARIPLA KMAVAESGMG 60 IVEDKVIKNH FASEYIYNAY KDEKTCGVLS EDDTFGTITI AEPIGIICGI VPTTNPTSTA 120 IFKSLISLKT RNAIIFSPHP RAKDATNKAA DIVLQAAIAA GAPKDLIGWI DQPSVELSNA 180 LMHHPDINLI LATGGPGMVK AAYSSGKPAI GVGAGNTPVV IDETADIKRA VASVLMSKTF 240 DNGVICASEQ SVVVVDSVYD AVRERFATHG GYLLQGKELK AVQDVILKNG ALNAAIVGQP 300 AYKIAELAGF SVPENTKILI GEVTVVDESE PFAHEKLSPT LAMYRAKDFE DAVEKAEKLV 360 AMGGIGHTSC LYTDQDNQPA RVSYFGQKMK TARILINTPA SQGGIGDLYN FKLAPSLTLG 420 CGSWGGNSIS ENVGPKHLIN KKTVAKRAEN MLWHKLPKSI YFRRGSLPIA LDEVITDGHK 480 RALIVTDRFL FNNGYADQIT SVLKAAGVET EVFFEVEADP TLSIVRKGAE LANSFKPDVI 540 IALGGGSPMD AAKIMWVMYE HPETHFEELA LRFMDIRKRI YKFPKMGVKA KMIAVTTTSG 600 TGSEVTPFAV VTDDATGQKY PLADYALTPD MAIVDANLVM DMPKSLCAFG GLDAVTHAME 660 AYVSVLASEF SDGQALQALK LLKEYLPASY HEGSKNPVAR ERVHSAATIA GIAFANAFLG 720 VCHSMAHKLG SQFHIPHGLA NALLICNVIR YNANDNPTKQ TAFSQYDRPQ ARRRYAEIAD 780 HLGLSAPGDR TAAKIEKLLA WLETLKAELG IPKSIREAGV QEADFLANVD KLSEDAFDDQ 840 CTGANPRYPL ISELKQILLD TYYGRDYVEG ETAAKKEAAP AKAEKKAKKS A 891 |
| GO:0008774 F:acetaldehyde dehydrogenase (acetylating) activity IEA:UniProtKB-EC GO:0004022 F:alcohol dehydrogenase (NAD) activity IEA:UniProtKB-EC GO:0046872 F:metal ion binding IEA:InterPro GO:0006066 P:alcohol metabolic process IEA:InterPro GO:0015976 P:carbon utilization IEA:InterPro |
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