Reviewed, UniProtKB/Swiss-Prot Q1INI5 (HEM12_ACIBL)

Names and origin

Protein names

Recommended name:
    Glutamyl-tRNA reductase 2
      Short name=GluTR 2
    EC=1.2.1.70

Gene names

Name:	hemA2
Ordered Locus Names:	Acid345_2564

Organism

Acidobacteria bacterium (strain Ellin345) [Complete proteome] [HAMAP]

Taxonomic identifier

204669 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Acidobacteriales › Acidobacteriaceae

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP MF_00087
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP 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.
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.
Sequence similarities	Belongs to the glutamyl-tRNA reductase family.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW porphyrin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: HAMAP shikimate 5-dehydrogenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 436	436	Glutamyl-tRNA reductase 2 HAMAP MF_00087		PRO_0000334999
Regions
	Nucleotide binding	186 – 191	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	111 – 113	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	106	1	Substrate By similarity
	Binding site	117	1	Substrate By similarity
	Site	96	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1INI5-1 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: 407B8A871D22A84C	FASTA	436	48,410
	10 20 30 40 50 60 MNFFVIGVNH KTAPVEVRER FAIPESRLPE ATKLLASYPG IEEGMIVSTC NRVEMVARSV 70 80 90 100 110 120 NGNADMRGFL KQLYNIDPAQ YEQYLYEYRS TEAVRHMFRV ASSLDSMVVG EPQILGQVKE 130 140 150 160 170 180 AYATARAVGA VSSQLDALLT RAFAVAKRVR TDTSIASSSV SIASVAVELA KKIFGSLQGR 190 200 210 220 230 240 SVYIVGAGKM CELAARHFVA HGVEKIYVAN RTYERGVAFA KKFNGEAVPI EHLYETVDKA 250 260 270 280 290 300 DIVLSSTGAP IAIFRKEHGE KFLSRRKNRP MFFLDIAVPR DVDAKMNELD GIFVYDIDDL 310 320 330 340 350 360 QQVVHSHISD RKDEAAHAEA IVNAEVEKFE ERLRTLDVVP TIVSLQEHLE TVRQAEIDRL 370 380 390 400 410 420 RGRLGELSPE QEMAVDALTK GIINKIMHTP ITTLKTAAKE PESTTVIELV KRIFNLHEKA 430 KDETVKTGPP QSGPGK

References

[1]

"Complete sequence of Acidobacteria bacterium Ellin345." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Kiss H., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Kuske C., Janssen P.H., Richardson P. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000360 Genomic DNA. Translation: ABF41565.1.
RefSeq	YP_591639.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4072208.
GenomeReviews	Gene locus Acid345_2564 in contig CP000360_GR.
KEGG	aba:Acid345_2564.
NMPDR	fig|204669.6.peg.2553.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1INI5.
OMA	Q1INI5. LLIDIAN.
Family and domain databases
HAMAP	MF_00087. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_C. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd_dom. IPR018214. pyrrol_synth_GluRdtase_CS. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
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.
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM12_ACIBL

Accession

Primary (citable) accession number: Q1INI5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	June 13, 2006
Last modified:	June 16, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)