Reviewed, UniProtKB/Swiss-Prot Q2IKT3 (HEM12_ANADE)

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:	Adeh_2493

Organism

Anaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]

Taxonomic identifier

290397 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Anaeromyxobacter

Protein attributes

Sequence length	446 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.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
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 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 – 446	446	Glutamyl-tRNA reductase 2		PRO_0000335006
Regions
	Nucleotide binding	185 – 190	6	NADP By similarity
	Region	53 – 56	4	Substrate binding By similarity
	Region	110 – 112	3	Substrate binding By similarity
Sites
	Active site	54	1	Nucleophile By similarity
	Binding site	105	1	Substrate By similarity
	Binding site	116	1	Substrate By similarity
	Site	95	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2IKT3-1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: B9DFB64DC19CB09C	FASTA	446	47,370
	10 20 30 40 50 60 MTGDRRLFLV GLSHKSAPID VRERVALTGD ALKAALCELK AMEGVTEALV VSTCNRVEVF 70 80 90 100 110 120 VHSDRPDAAR RFFTERSPAA ADHLYAKDGV EAVRHLFRVA SSLDSMVVGE QQILGQVKEA 130 140 150 160 170 180 YGLASAASAA GSYFSRLCNR AFATAKRVRT ETEIGRGATS MSQVAVELVE KIFGRLEGRA 190 200 210 220 230 240 ILLVGAGKMG ALSAKALAVL GADRILVTNR SPERGLALAA QVSGSYRGWE ELQRLLGEAD 250 260 270 280 290 300 VVIVSTGAPT YVVTRESMHA AMKARRRRSI CLIDLAVPRN VDPACAELSD VYAYDVDDME 310 320 330 340 350 360 RVVATSKQAR QGEAIRAEAI VEAEVMAFAK EREARAALPV LAQLRRHAER IARAEAERTL 370 380 390 400 410 420 AQVGGKLDDK GRKSVEAMAQ AIVNKLLHGP TSRLKEAASS GDSALPGAAA ELFGIENETA 430 440 GGERREGGAE GAAAAPGAGP VRSQGT

References

[1]

"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000251 Genomic DNA. Translation: ABC82263.1.
RefSeq	YP_465700.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3890055.
GenomeReviews	Gene locus Adeh_2493 in contig CP000251_GR.
KEGG	ade:Adeh_2493.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2IKT3.
Enzyme and pathway databases
BioCyc	ADEH290397:ADEH_2493-MON.
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. IPR006151. Shikm_DHase/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_ANADE

Accession

Primary (citable) accession number: Q2IKT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	March 7, 2006
Last modified:	November 25, 2008
This is version 32 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)