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UniProtKB/Swiss-Prot entry P43876

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AROE_HAEIN
Primary accession number P43876
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 66)
Name and origin of the protein
Protein name Shikimate dehydrogenase
Synonym EC 1.1.1.25
Gene name
Name: aroE
OrderedLocusNames: HI0655
From
Haemophilus influenzae [TaxID: 727] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Haemophilus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
PubMed=7542800 [NCBI, ExPASy, EBI, Israel, Japan]
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd.";
Science 269:496-512(1995).
[2]
 X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT.
DOI=10.1128/JB.185.14.4144-4151.2003; PubMed=12837789 [NCBI, ExPASy, EBI, Israel, Japan]
Ye S., Von Delft F., Brooun A., Knuth M.W., Swanson R.V., McRee D.E.;
"The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode.";
J. Bacteriol. 185:4144-4151(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L42023; AAC22314.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H64084; H64084.
RefSeq NP_438815.1; -.
3D structure databases
PDB
1P74; X-ray; 2.40 A; A/B=1-272.[ExPASy / RCSB / EBI]
1P77; X-ray; 1.95 A; A=1-272.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1P74; -.
1P77; -.
ModBase P43876.
Enzyme and pathway databases
BioCyc HINF71421:HI_0655-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0004764; Molecular function: shikimate 5-dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0009073; Biological process: aromatic amino acid family biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_00222; -; 1.
PBIL [Tree]
InterPro IPR016040; NAD(P)-bd.
IPR011342; Quinate/shikimate_5-DHase.
IPR013708; Shikimate_DHase-bd_N.
IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF01488; Shikimate_DH; 1.
PF08501; Shikimate_dh_N; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00507; aroE; 1.
ProtoNet P43876.
Genome annotation databases
GeneID 949697; -.
GenomeReviews L42023_GR; HI0655.
KEGG hin:HI0655; -.
NMPDR fig|71421.1.peg.625; -.
TIGR HI0655; -.
Phylogenomic databases
HOGENOM P43876; -.
Other
LinkHub P43876; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Complete proteome; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   272  272     Shikimate dehydrogenase. PRO_0000136006
NP_BIND   126   130  5     NADP. 
NP_BIND   149   154  6     NADP. 
NP_BIND   238   242  5     NADP (By similarity). 
ACT_SITE   65    65        Proton acceptor (Potential). 
BINDING   102   102        Substrate (By similarity). 
BINDING   189   189        NADP; via amide nitrogen. 
BINDING   190   190        NADP; via amide nitrogen. 
STRAND   2    10  9      
HELIX   16    26  11      
STRAND   31    37  7      
TURN   40    42  3      
HELIX   43    52  10      
STRAND   57    60  4      
HELIX   65    69  5      
STRAND   73    75  3      
HELIX   77    82  6      
STRAND   86    90  5      
STRAND   92    94  3      
STRAND   96    99  4      
HELIX   102   112  11      
STRAND   121   126  6      
HELIX   129   134  6      
HELIX   135   140  6      
STRAND   144   150  7      
HELIX   154   162  9      
HELIX   163   165  3      
STRAND   168   172  5      
STRAND   181   186  6      
HELIX   201   204  4      
STRAND   210   213  4      
STRAND   217   219  3      
HELIX   222   229  8      
HELIX   239   254  16      
HELIX   260   269  10      
Sequence information
Length: 272 AA [This is the length of the unprocessed precursor] Molecular weight: 29760 Da [This is the MW of the unprocessed precursor] CRC64: 3B7A92AF22D4470B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDLYAVWGNP IAQSKSPLIQ NKLAAQTHQT MEYIAKLGDL DAFEQQLLAF FEEGAKGCNI 

        70         80         90        100        110        120 
TSPFKERAYQ LADEYSQRAK LAEACNTLKK LDDGKLYADN TDGIGLVTDL QRLNWLRPNQ 

       130        140        150        160        170        180 
HVLILGAGGA TKGVLLPLLQ AQQNIVLANR TFSKTKELAE RFQPYGNIQA VSMDSIPLQT 

       190        200        210        220        230        240 
YDLVINATSA GLSGGTASVD AEILKLGSAF YDMQYAKGTD TPFIALCKSL GLTNVSDGFG 

       250        260        270 
MLVAQAAHSF HLWRGVMPDF VSVYEQLKKA ML
P43876 in FASTA format

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