Reviewed, UniProtKB/Swiss-Prot O08393 (HEM1_ANASP)

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:	alr1042

Organism

Anabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]

Taxonomic identifier

103690 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc

Protein attributes

Sequence length	428 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 Porphyrin biosynthesis; chlorophyll biosynthesis. 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	Chlorophyll biosynthesis Porphyrin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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 – 428	428	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_0000113986
Regions
	Nucleotide binding	189 – 194	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	114 – 116	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	109	1	Substrate By similarity
	Binding site	120	1	Substrate By similarity
	Site	99	1	Important for activity By similarity
Experimental info
	Sequence conflict	33	1	A → G in AAB58164. Ref.1
	Sequence conflict	48	1	S → G in AAB58164. Ref.1
	Sequence conflict	174	1	Q → E in AAB58164. Ref.1
	Sequence conflict	280	1	I → V in AAB58164. Ref.1
	Sequence conflict	374 – 380	7	DKHQEVI → EQTSRGV in AAB58164. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O08393-1 [UniParc]. Last modified January 23, 2002. Version 2. Checksum: 06A470955F9D3C64	FASTA	428	47,909
	10 20 30 40 50 60 MNIAVVGLSH KTAPVEIREK LSIPEPQTES AIAQLTSYPH IDEVAILSTC NRLEIYIVAG 70 80 90 100 110 120 ETDHGIREVT QFLSEHSKLP VHSLRQHLFV LLHEDAVMHI MRVAAGLDSL VLGEGQILAQ 130 140 150 160 170 180 VKNTHKLGQQ YNGIKTILNR LFKQALTAGK RVRTETSIGT GAVSISSAAV ELAQIKAENL 190 200 210 220 230 240 AACRVTILGA GKMSRLLVQH LVSKGATQIS IVNRSRERAQ ELAKQFSEHP IRTHLLPEMM 250 260 270 280 290 300 TVIAESHLVF TSTSATEPIL DRAKLEMVLA PNQPLMLFDI SVPRNVHTDV NELVNVQAFN 310 320 330 340 350 360 VDDLKAVVAQ NYESRRKMAQ EAERLLEEEI EAFDIWWRSL ETVSTISSLR SKIETIREQE 370 380 390 400 410 420 LEKALSRLGS EFGDKHQEVI EALTRGIVNK ILHDPMVQLR AQQDVEARRR CMQTLQMLFN LDVGEQFS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of hemA, a gene encoding glutamyl tRNA reductase in the cyanobacterium Anabaena sp. strain 7120." Woelfle M.A., Haselkorn R. Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120." Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. , Takazawa M., Yamada M., Yasuda M., Tabata S. DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	U97695 Genomic DNA. Translation: AAB58164.1. BA000019 Genomic DNA. Translation: BAB72999.1.
PIR	AG1936.
RefSeq	NP_485085.1.
3D structure databases
HSSP	HSSP built from PDB template 1GPJ based on UniProtKB Q9UXR8.
ModBase	Search...
Genome annotation databases
GeneID	1104636.
GenomeReviews	Gene locus alr1042 in contig BA000019_GR.
KEGG	ana:alr1042.
NMPDR	fig|103690.1.peg.1352.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O08393.
OMA	O08393. GPILNRL.
Enzyme and pathway databases
BioCyc	NSP103690:ALR1042-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_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_ANASP

Accession

Primary (citable) accession number: O08393

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2002
Last modified:	June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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