Tag | Content |
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CPLM ID | CPLM-002416 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Histidinol dehydrogenase |
Protein Synonyms/Alias | HDH |
Gene Name | hisD |
Gene Synonyms/Alias | b2020; JW2002 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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44 | NDILDNVKARGDEAL | acetylation | [1] | 57 | ALREYSAKFDKTTVT | acetylation | [1] | 60 | EYSAKFDKTTVTALK | acetylation | [1] | 85 | ERLSDELKQAMAVAV | acetylation | [1] | 93 | QAMAVAVKNIETFHT | acetylation | [1] | 103 | ETFHTAQKLPPVDVE | acetylation | [1] | 397 | MTVQELSKEGFSALA | acetylation | [1] | 420 | AERLTAHKNAVTLRV | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. |
Sequence Annotation | ACT_SITE 326 326 Proton acceptor. ACT_SITE 327 327 Proton acceptor. METAL 259 259 Zinc. METAL 262 262 Zinc. METAL 360 360 Zinc. METAL 419 419 Zinc. BINDING 130 130 NAD. BINDING 188 188 NAD. BINDING 211 211 NAD. BINDING 237 237 Substrate. BINDING 259 259 Substrate. BINDING 262 262 Substrate. BINDING 327 327 Substrate. BINDING 360 360 Substrate. BINDING 414 414 Substrate. BINDING 419 419 Substrate. |
Keyword | 3D-structure; Amino-acid biosynthesis; Complete proteome; Direct protein sequencing; Histidine biosynthesis; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 434 AA |
Protein Sequence | MSFNTIIDWN SCTAEQQRQL LMRPAISASE SITRTVNDIL DNVKARGDEA LREYSAKFDK 60 TTVTALKVSA EEIAAASERL SDELKQAMAV AVKNIETFHT AQKLPPVDVE TQPGVRCQQV 120 TRPVASVGLY IPGGSAPLFS TVLMLATPAS IAGCKKVVLC SPPPIADEIL YAAQLCGVQD 180 VFNVGGAQAI AALAFGTESV PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL 240 VIADSGATPD FVASDLLSQA EHGPDSQVIL LTPAADMARR VAEAVERQLA ELPRAETARQ 300 ALNASRLIVT KDLAQCVEIS NQYGPEHLII QTRNARELVD SITSAGSVFL GDWSPESAGD 360 YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKEGF SALASTIETL AAAERLTAHK 420 NAVTLRVNAL KEQA 434 |
Gene Ontology | GO:0004399; F:histidinol dehydrogenase activity; IDA:EcoCyc. GO:0051287; F:NAD binding; IEA:InterPro. GO:0008270; F:zinc ion binding; IEA:HAMAP. GO:0000105; P:histidine biosynthetic process; IDA:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |