B9LR55 (B9LR55_HALLT) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Glutamyl-tRNA reductase HAMAP MF_00087
Short name=GluTR HAMAP MF_00087
EC=1.2.1.70 HAMAP MF_00087

Gene names

Name:	hemA HAMAP MF_00087
Ordered Locus Names:	Hlac_2132

Organism

Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34) [Complete proteome] [HAMAP]

Taxonomic identifier

416348 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Halorubrum

Protein attributes

Sequence length	447 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 MF_00087
Catalytic activity	L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP MF_00087 RuleBase RU000584
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP MF_00087 RuleBase RU000584
Subunit structure	Homodimer By similarity. HAMAP MF_00087
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 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 MF_00087
Sequence similarities	Belongs to the glutamyl-tRNA reductase family. HAMAP MF_00087 RuleBase RU000584

Ontologies

Keywords
Biological process	Porphyrin biosynthesis HAMAP MF_00087 RuleBase RU000584
Ligand	NADP HAMAP MF_00087 RuleBase RU000584
Molecular function	Oxidoreductase HAMAP MF_00087 RuleBase RU000584 EMBL ACM57709.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: HAMAP
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
Regions
	Nucleotide binding	183 – 188	6	NADP By similarity HAMAP MF_00087
	Region	51 – 54	4	Substrate binding By similarity HAMAP MF_00087
	Region	109 – 111	3	Substrate binding By similarity HAMAP MF_00087
Sites
	Active site	52	1	Nucleophile By similarity HAMAP MF_00087
	Binding site	104	1	Substrate By similarity HAMAP MF_00087
	Binding site	115	1	Substrate By similarity HAMAP MF_00087
	Site	94	1	Important for activity By similarity HAMAP MF_00087

Sequences

	Sequence		Length	Mass (Da)
	B9LR55 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: 59B0EF5260E00D49	FASTA	447	47,337
	10 20 30 40 50 60 MKETGAITGI SVAYSRATVD EIEAAGGDGV RATVSDLLAR DGVEEAFAIQ TCNRSEAYVV 70 80 90 100 110 120 TDRTIDGSVA LESFAPEVRG GAVRRLDHEE SLEHLMRVAS GLESLVLGED QIIGQLREAY 130 140 150 160 170 180 EESKSAGGIG PVLKDGVTKA LHVGERARNE TSINEGVVSL GSAAVRLAAD EIDLTDGSAV 190 200 210 220 230 240 VVGAGEMGTL AARTLDDTPV SEIVVANRTV PNAAFVAEEV ETPAEAVPLA DLATVIPDAD 250 260 270 280 290 300 LVIAATGSPD PVIRSEHVTG ADRLVCIDIA QPRDIEPALA DRDKVTLYDI DALEDVTRKT 310 320 330 340 350 360 RESREEEARE VEAIIDEELD RILEAYKRKR ADNAISAMYA GADRVKAREV DRAVSKLEAQ 370 380 390 400 410 420 GGLTDEQRET VEDLADALVG QLLAAPTRSL RDAAGEDDWE TIRTALRLFD PEFDTLPEGP 430 440 GASGSGHDAA PGDIEVPPGS VAEELDD

References

[1]

"Complete sequence of chromosome1 of Halorubrum lacusprofundi ATCC 49239." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N. , Anderson I., DasSarma S., Cavicchioli R., Richardson P. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001365 Genomic DNA. Translation: ACM57709.1.
RefSeq	YP_002566779.1. NC_012029.1.
3D structure databases
ProteinModelPortal	B9LR55.
ModBase	Search...
Protein-protein interaction databases
STRING	B9LR55.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7400652.
GenomeReviews	Gene locus Hlac_2132 in contig CP001365_GR.
KEGG	hla:Hlac_2132.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	ERCLREC.
ProtClustDB	PRK00045.
Family and domain databases
HAMAP	MF_00087. Glu_tRNA_reductase. [Tree]
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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K02492.
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

B9LR55_HALLT

Accession

Primary (citable) accession number: B9LR55

Entry history

Integrated into UniProtKB/TrEMBL:	March 24, 2009
Last sequence update:	March 24, 2009
Last modified:	December 14, 2011
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)