Reviewed, UniProtKB/Swiss-Prot A8MGE1 (HEM1_ALKOO)

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:	Clos_1324

Organism

Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OhILAs)) [Complete proteome] [HAMAP]

Taxonomic identifier

350688 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Alkaliphilus

Protein attributes

Sequence length	334 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 – 334	334	Glutamyl-tRNA reductase		PRO_1000057568
Regions
	Nucleotide binding	186 – 191	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	112 – 114	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	107	1	Substrate By similarity
	Binding site	118	1	Substrate By similarity
	Site	97	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8MGE1-1 [UniParc]. Last modified December 4, 2007. Version 1. Checksum: 8F26F7A9D7D44A9F	FASTA	334	38,048
	10 20 30 40 50 60 MNIIMAGIDY KLAPIDVREG FSFTKAMMKQ VYSNILKDTM IYGTVIISTC NRTEIYISCE 70 80 90 100 110 120 EDFCVNPFEV LCNAAGIDFT PYEKVHRVKE GDEVIKHLCQ LACGVKSQIW GEDQIITQVK 130 140 150 160 170 180 NAIAVSREMR AADSYLEVMF RNAIAAAKKV KSTLILNSRE NSIVHKALKI IKDQETMNIR 190 200 210 220 230 240 EILVIGNGEM GRLMTNVLIE NGYRATMTLR QYRYHANVIP LNANTVDYSN RYEKMKDCDV 250 260 270 280 290 300 VISATLSPHY TVEMENLKKI DKIPKLFIDL AVPRDIDPSI KNLPNIELYD VDGIGADEIS 310 320 330 KNHAQQLKGI ERIIEKYICD YHKWCLFKEG LGCI

References

[1]

"Complete genome of Alkaliphilus oremlandii OhILAs." 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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000853 Genomic DNA. Translation: ABW18869.1.
RefSeq	YP_001512865.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5677168.
GenomeReviews	Gene locus Clos_1324 in contig CP000853_GR.
KEGG	aoe:Clos_1324.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_00087. [Tree]
InterPro	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	PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. [Graphical view]
PROSITE	PS00747. GLUTR. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_ALKOO

Accession

Primary (citable) accession number: A8MGE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	December 4, 2007
Last modified:	November 25, 2008
This is version 9 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)