Glutamyl-tRNA reductase - Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)

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Q5N3B4 (HEM1_SYNP6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glutamyl-tRNA reductase
Short name=GluTR
EC=1.2.1.70

Gene names

Name:	hemA
Ordered Locus Names:	syc1016_d

Organism

Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP]

Taxonomic identifier

269084 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus ›

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity. HAMAP-Rule MF_00087
Catalytic activity	L-glutamate 1-semialdehyde + NADP⁺ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP-Rule MF_00087
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP-Rule MF_00087 Porphyrin biosynthesis; chlorophyll biosynthesis. HAMAP-Rule MF_00087
Subunit structure	Homodimer By similarity.
Domain	Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization By similarity. HAMAP-Rule MF_00087
Miscellaneous	During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA By similarity. HAMAP-Rule MF_00087
Sequence similarities	Belongs to the glutamyl-tRNA reductase family.

Ontologies

Keywords
Biological process	Chlorophyll biosynthesis Porphyrin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: HAMAP protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	NADP binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 438

438

Glutamyl-tRNA reductase HAMAP-Rule MF_00087

PRO_1000004709

Regions

Nucleotide binding

197 – 202

NADP By similarity

Region

49 – 52

Substrate binding By similarity

Region

114 – 116

Substrate binding By similarity

Sites

Active site

Nucleophile By similarity

Binding site

109

Substrate By similarity

Binding site

120

Substrate By similarity

Site

Important for activity By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q5N3B4 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: A43002486A81F746
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FASTA

438

48,445

        10         20         30         40         50         60 
MHLAVVGLSH RTAPVAVREK LSIPEQQVEA AIQQLKSYPH IEEVAILSTC NRLEIYCVTR 

        70         80         90        100        110        120 
ATEPGVREIT QFLSEHSHLP LGELRPHLFV LLHQDAVMHL MRVAAGLDSL VLGEGQILSQ 

       130        140        150        160        170        180 
VKTMYKLGQQ YEGVGRILNR LLKQAVTAGK RVRTETSIGT GAVSISSAAV ELAQLKVIAR 

       190        200        210        220        230        240 
DDRSDGNLAG QRVLILGAGK MSRLLVQHLI AKGADTIQIL NRTLGRAEEL AKQYGGDLQI 

       250        260        270        280        290        300 
QVGLLSGLMN AIVEADIVFT STSATDPILD RAKLEMVLAP EQRLMLIDIA VPRNVAADVV 

       310        320        330        340        350        360 
ELTSVESYNV DDLREVVAQN QESRRKLAEE AEALLEEEVD AFDNWWQSLD TVPTINCLRD 

       370        380        390        400        410        420 
KIEMIREQEL EKALSRLGTE FGDKHQAVVE ALTRGIVNKI LHDPMVQLRS QQDIEARRRA 

       430 
VDALQMLFNL DPQGQLSS

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References

[1]

"Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP008231 Genomic DNA. Translation: BAD79206.1.
RefSeq	YP_171726.1. NC_006576.1.
3D structure databases
HSSP	HSSP built from PDB template 1GPJ based on UniProtKB Q9UXR8.
ProteinModelPortal	Q5N3B4.
ModBase	Search...
Protein-protein interaction databases
STRING	269084.syc1016_d.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAD79206; BAD79206; syc1016_d.
GeneID	3199869.
KEGG	syc:syc1016_d.
PATRIC	32487844. VBISynElo117686_1182.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0373.
HOGENOM	HOG000109651.
KO	K02492.
OMA	GPILNRL.
ProtClustDB	PRK00045.
Enzyme and pathway databases
UniPathway	UPA00251; UER00316. UPA00668.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_00087. Glu-tRNA_reductase.
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_dimer. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd_dom. IPR018214. Pyrrol_synth_GluRdtase_CS. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view]
Pfam	PF00745. GlutR_dimer. 1 hit. PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. [Graphical view]
PIRSF	PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAM	SSF69075. 4pyrrol_synth_GluRdtase_C. 1 hit. SSF69742. GlutR. 1 hit.
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_SYNP6

Accession

Primary (citable) accession number: Q5N3B4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 1, 2005
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents