ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P49294


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name HEM12_ARATH
Primary accession number P49294
Secondary accession numbers O04950 Q0WQP1 Q4V3B7
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on July 24, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 69)
Name and origin of the protein
Protein name Glutamyl-tRNA reductase 2, chloroplastic [Precursor]
Synonyms GluTR
EC 1.2.1.70
Gene name
Name: HEMA2
OrderedLocusNames: At1g09940
ORFNames: F21M12.33
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], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
DOI=10.1007/BF00049321; PubMed=8605295 [NCBI, ExPASy, EBI, Israel, Japan]
Kumar A.M., Csankovszki G., Soell D.;
"A second and differentially expressed glutamyl-tRNA reductase gene from Arabidopsis thaliana.";
Plant Mol. Biol. 30:419-426(1996).
[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;
Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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
U27118; AAB01674.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC000132; AAB60749.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT023439; AAY56430.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK228651; BAF00558.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G86233; G86233.
S65773; S65773.
RefSeq NP_172465.1; -.
UniGene At.27711
3D structure databases
HSSP Q9UXR8; 1GPJ. [HSSP ENTRY / PDB]
ModBase P49294.
Enzyme and pathway databases
BioCyc MetaCyc:AT1G09940-MON; -.
Organism-specific databases
TAIR At1g09940; -.
Gene expression databases
ArrayExpress P49294; -.
GermOnline AT1G09940; Arabidopsis thaliana.
Family and domain databases
InterPro IPR000343; 4pyrrol_synth_GluRdtase.
IPR015896; 4pyrrol_synth_GluRdtase_C.
IPR015895; 4pyrrol_synth_GluRdtase_N.
IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
Graphical view of domain structure.
Pfam PF00745; GlutR_dimer; 1.
PF05201; GlutR_N; 1.
PF01488; Shikimate_DH; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000445; 4pyrrol_synth_GluRdtase; 1.
TIGRFAMs TIGR01035; hemA; 1.
PROSITE PS00747; GLUTR; 1.
BLOCKS P49294.
Genome annotation databases
GeneID 837528; -.
GenomeReviews CT485782_GR; AT1G09940.
KEGG ath:AT1G09940; -.
NMPDR fig|3702.1.peg.1230; -.
Other
ProtoNet P49294.
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    64  64     Chloroplast (Potential). 
CHAIN   65   530  466     Glutamyl-tRNA reductase 2, chloroplastic. PRO_0000013308
NP_BIND   277   282  6     NADP (By similarity). 
REGION   134   137  4     Substrate binding (By similarity). 
REGION   199   201  3     Substrate binding (By similarity). 
ACT_SITE   135   135        Nucleophile (By similarity). 
BINDING   194   194        Substrate (By similarity). 
BINDING   205   205        Substrate (By similarity). 
SITE   184   184  1     Important for activity (By similarity). 
CONFLICT   245   245        A -> G (in Ref. 4; BAF00558). 
CONFLICT   410   410        D -> E (in Ref. 1; AAB01674). 
Sequence information
Length: 530 AA [This is the length of the unprocessed precursor] Molecular weight: 58292 Da [This is the MW of the unprocessed precursor] CRC64: 0C0224296BA3D0A8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVSSAFVVT PKLEKLLANH HNPTYSSSPA PLDVIGIRAL PMNNRNKRGL IQRARCEISP 

        70         80         90        100        110        120 
SNKAASISAL EQLKTSAIDR YTKERSSIVV IGLSIHTAPV EMREKLAIPE AEWPRAIAEL 

       130        140        150        160        170        180 
CGLNHIEEAA VLSTCNRMEI YVLALSQHRG VKEVTEWMSK TSGIPVSEIC QHRFLLYNKD 

       190        200        210        220        230        240 
VTQHIFEVSA GLDSLVLGEG QILAQVKQVV KVGQGVNGFG RNISGLFKHA ITVGKRVRTE 

       250        260        270        280        290        300 
TNIAAGAVSV SSAAVELALM KLPESSHASS ARMLVVGAGK MGKLVIKHLV AKGCTKMVVV 

       310        320        330        340        350        360 
NRSEEKVAAV RNEMPPGVEI IYKPLDEMLS CAAEADVVFT STASETPLFL KEQVETLPPV 

       370        380        390        400        410        420 
RDARLFVDIS VPRNVGSCVA EIDGTRVFNV DDLKEVVAAN KEDRVRKAMD AQAIITDESK 

       430        440        450        460        470        480 
HFEAWRDSLE TVPTIKKLRG YTERIIAAEI EKSLPKMGID MNKKMRKTVD DLIRGIVNKL 

       490        500        510        520        530 
LHGPMQHLRC DGNDSRTLSE TLDNMQALNR MYGLDAEILE EKIRAKVEKK 

P49294 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!