Reviewed, UniProtKB/Swiss-Prot A1K442 (HEM1_AZOSB)

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:	azo0980

Organism

Azoarcus sp. (strain BH72) [Complete proteome] [HAMAP]

Taxonomic identifier

62928 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Azoarcus

Protein attributes

Sequence length	417 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 – 417	417	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_1000004593
Regions
	Nucleotide binding	185 – 190	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	110 – 112	3	Substrate binding By similarity
Sites
	Active site	50	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)
	A1K442-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 987D9E7289CC26F0	FASTA	417	45,646
	10 20 30 40 50 60 MQLYALGLNH HTAPLAIRER VAFQPDRLDQ ALQALTDSRT VSEAAILSTC NRTELYFAAE 70 80 90 100 110 120 QPQRAADWLA GFHQLPLAQV SPYLYSYPQR DAVRHVFRVA SGLDSMVLGE PQILGQVKEA 130 140 150 160 170 180 ARRAEEAGTL GTLLHKLFQN TFAVAKEVRS TTAIGANIVS MAAAAVHLTG RIFERVSDQH 190 200 210 220 230 240 VLFIGAGEMI ELCAAHFAGA GPRSMTVANR TEARAEALAA RLGAQTMRLD AIADALPRFD 250 260 270 280 290 300 VVVSCTASPL PIVGLGMVER AVKVRRHRPI VMVDLAVPRD VEPEVGQLDD VFLYTVDDLA 310 320 330 340 350 360 QVVDAGIESR QQAVVEAEGI IDQRVDGFLH WLHARDAVPT IRALREHAET LRRGEIERAL 370 380 390 400 410 RQLAKGEDPQ AVLDALSHGL TNKLMHGPTR FLTQAEGEGQ AEASRVVQQL FNLSRHD

References

[1]

"Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. strain BH72." Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., Weidner S. , Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A. Nat. Biotechnol. 24:1385-1391(2006) [PubMed: 17057704] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM406670 Genomic DNA. Translation: CAL93597.1.
RefSeq	YP_932484.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4610012.
GenomeReviews	Gene locus azo0980 in contig AM406670_GR.
KEGG	azo:azo0980.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A1K442. GPILNRL.
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

HEM1_AZOSB

Accession

Primary (citable) accession number: A1K442

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 6, 2007
Last modified:	June 16, 2009
This is version 23 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)