Q2JJG8 (HEM1_SYNJB) Reviewed, UniProtKB/Swiss-Prot

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:	CYB_2258

Organism

Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime) [Complete proteome] [HAMAP]

Taxonomic identifier

321332 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus

Protein attributes

Sequence length	431 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 – 431	431	Glutamyl-tRNA reductase HAMAP-Rule MF_00087		PRO_1000004708
Regions
	Nucleotide binding	189 – 194	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	114 – 116	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	109	1	Substrate By similarity
	Binding site	120	1	Substrate By similarity
	Site	99	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2JJG8 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: C34C228554FDB259	FASTA	431	48,026
	10 20 30 40 50 60 MFIAVVGLSH RTAPVEIRER LSIAEAEVGE TIQQLRTHPH IEEAAILSTC NRLEVYIVTS 70 80 90 100 110 120 EMESGVRQTM QFLAELKGIP LPQLRPHLFT LLYQDAVTHL MRVAAGLDSL VLGEGQILSQ 130 140 150 160 170 180 VKKAQQLGQA CNGMDRILNR LFKAAITAGK RVRTETEIGT GAMSISSAAV ELALQEQGSL 190 200 210 220 230 240 SQGKVTVVGA GRMARLLVQH LLAKGAVDIT VVNRSLERAE ALAKQFEQPI QVLPWESLLN 250 260 270 280 290 300 SVAESNLVFT STGATQPILN YQQLAGVLQP DQPLLLVDIS VPRNIDPDVE KLKGVQVFNV 310 320 330 340 350 360 DHLSRIVEEN RAQRQKLALA AEALVEEEVD QFMEWWRSLE TVPTISSLRH KVESIREQEM 370 380 390 400 410 420 EKALSRLGKD FAEKHLEVID ALTRGIVNKI LHDPMVQLRA KRDIEARRAA MRILQELFNL 430 DPVVFQAQQE R

References

[1]

"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses." Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F. ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JA-2-3B'a(2-13).

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000240 Genomic DNA. Translation: ABD03199.1.
RefSeq	YP_478462.1. NC_007776.1.
3D structure databases
ProteinModelPortal	Q2JJG8.
ModBase	Search...
Protein-protein interaction databases
STRING	321332.CYB_2258.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABD03199; ABD03199; CYB_2258.
GeneID	3900421.
KEGG	cyb:CYB_2258.
PATRIC	23806866. VBISynSp29577_2262.
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_SYNJB

Accession

Primary (citable) accession number: Q2JJG8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program