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UniProtKB/Swiss-Prot entry P42804


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

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Entry information
Entry name HEM11_ARATH
Primary accession number P42804
Secondary accession number Q9LQB9
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on April 3, 2002 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 72)
Name and origin of the protein
Protein name Glutamyl-tRNA reductase 1, chloroplastic [Precursor]
Synonyms GluTR
EC 1.2.1.70
Gene name
Name: HEMA1
Synonyms: HEMA
OrderedLocusNames: At1g58290
ORFNames: F19C14.9
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=cv. Columbia;
TISSUE=Leaf;
DOI=10.1105/tpc.6.2.265; PubMed=7908550 [NCBI, ExPASy, EBI, Israel, Japan]
Ilag L.L., Kumar A.M., Soell D.;
"Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis.";
Plant Cell 6:265-275(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(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
U03774; AAA19118.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC008051; AAF82258.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY072223; AAL60044.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY096600; AAM20250.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E96616; E96616.
RefSeq NP_176125.1; -.
UniGene At.241
3D structure databases
HSSP Q9UXR8; 1GPJ. [HSSP ENTRY / PDB]
ModBase P42804.
Enzyme and pathway databases
BioCyc MetaCyc:AT1G58290-MON; -.
Organism-specific databases
TAIR At1g58290; -.
Gene expression databases
ArrayExpress P42804; -.
GermOnline AT1G58290; Arabidopsis thaliana.
Family and domain databases
InterPro IPR000343; 4pyrrol_synth_GluRdtase.
IPR015896; 4pyrrol_synth_GluRdtase_C.
IPR015895; 4pyrrol_synth_GluRdtase_N.
IPR016040; NAD(P)-bd.
IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00745; GlutR_dimer; 1.
PF05201; GlutR_N; 1.
PF01488; Shikimate_DH; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01035; hemA; 1.
PROSITE PS00747; GLUTR; 1.
BLOCKS P42804.
Genome annotation databases
GeneID 842198; -.
GenomeReviews CT485782_GR; AT1G58290.
KEGG ath:AT1G58290; -.
NMPDR fig|3702.1.peg.5290; -.
Other
ProtoNet P42804.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chlorophyll biosynthesis; Chloroplast; Complete proteome; NADP; Oxidoreductase; Plastid; Porphyrin biosynthesis; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Chloroplast (Potential). 
CHAIN   ?   543        Glutamyl-tRNA reductase 1, chloroplastic. PRO_0000013307
NP_BIND   285   290  6     NADP (By similarity). 
REGION   143   146  4     Substrate binding (By similarity). 
REGION   208   210  3     Substrate binding (By similarity). 
COMPBIAS   23    33  11     Poly-Ser. 
COMPBIAS   305   308  4     Poly-Val. 
ACT_SITE   144   144        Nucleophile (By similarity). 
BINDING   203   203        Substrate (By similarity). 
BINDING   214   214        Substrate (By similarity). 
SITE   193   193  1     Important for activity (By similarity). 
CONFLICT   62    62        E -> V (in Ref. 1; AAA19118). 
CONFLICT   169   169        K -> N (in Ref. 1; AAA19118). 
CONFLICT   291   291        K -> L (in Ref. 1; AAA19118). 
CONFLICT   542   542        Q -> H (in Ref. 1; AAA19118). 
Sequence information
Length: 543 AA [This is the length of the unprocessed precursor] Molecular weight: 59515 Da [This is the MW of the unprocessed precursor] CRC64: 04A095FEC96CC014 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVSSAFVGC PKLETLLNHH NLSPSSSSSS SVSQTPLGLN GVRVLPKNNR TRRGLIQKAR 

        70         80         90        100        110        120 
CELSASSDSA SNAASISALE QLKNSAADRY TKERSSIVVI GLSIHTAPVE MREKLAIPEA 

       130        140        150        160        170        180 
EWPRAIAELC GLNHIEEAAV LSTCNRMEIY VLALSQHRGV KEVTEWMSKT SGIPVSEICQ 

       190        200        210        220        230        240 
HRFLLYNKDA TQHIFEVSAG LDSLVLGEGQ ILAQVKQVVK VGQGVNGFGR NISGLFKHAI 

       250        260        270        280        290        300 
TVGKRVRTET NIASGAVSVS SAAVELALMK LPQSSNVSAR MCVIGAGKMG KLVIKHLMAK 

       310        320        330        340        350        360 
GCTKVVVVNR SEERVSAIRE EMPGIEIIYR PLDEMLACAS EADVVFTSTA SETPLFLKEH 

       370        380        390        400        410        420 
VENLPQASPE VGGLRHFVDI SVPRNVGSCV GEVETARVYN VDDLKEVVAA NKEDRMRKAM 

       430        440        450        460        470        480 
EAQTIITEES TQFEAWRDSL ETVPTIKKLR AYAERIRVAE LEKCMSKMGD DINKKTTRAV 

       490        500        510        520        530        540 
DDLSRGIVNR FLHGPMQHLR CDGSDSRTLS ETLENMHALN RMYGLEKDIL EEKLKAMAEQ 


QQK 

P42804 in FASTA format

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