Reviewed, UniProtKB/Swiss-Prot A0JYN2 (HEM1_ARTS2)

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:	Arth_2773

Organism

Arthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]

Taxonomic identifier

290399 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

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. 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 – 446	446	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_0000335010
Regions
	Nucleotide binding	192 – 197	6	NADP By similarity
	Region	47 – 50	4	Substrate binding By similarity
	Region	115 – 117	3	Substrate binding By similarity
Sites
	Active site	48	1	Nucleophile By similarity
	Binding site	110	1	Substrate By similarity
	Binding site	121	1	Substrate By similarity
	Site	100	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0JYN2-1 [UniParc]. Last modified May 20, 2008. Version 2. Checksum: E50D8052A049F03E	FASTA	446	46,394
	10 20 30 40 50 60 MVLFSLVATH ADIDLETVAQ LSTGASELAT SALSGSPAVK GAVVLATCNR FEIYGEAPHP 70 80 90 100 110 120 DDVEAARAAL VAQISERTGL NEQLVSRSFN TRTGGEVSQH LFAVSSGLDS AVVGEREIAG 130 140 150 160 170 180 QVRRALINAQ HEGTASSGLV RLFQAASKTA KDVGAQTALG SRGLSIVSVA LDLATDLSEN 190 200 210 220 230 240 PDWSAKKAVV FGTGAYAGAT MSLLRERGCT DISVFSSSGR AEGFVATRGG KALDSDTLPA 250 260 270 280 290 300 AVAAADVMIG CSGSDTRVEA EELARVRAGS AQTLIAIDLA LTHDFDPAVG ELDGVELLTL 310 320 330 340 350 360 ESVRLAAPQE QAESLAQASG IVTGAAAAFE QEREARSVDS AIVALRRHTM NVLDAEMEKV 370 380 390 400 410 420 RARHGCTAAA EEVEFALRRM VKQLLHVPTV RARELASNGQ QEQYIAALDA LYGITVEQPA 430 440 AAPAAECPVD HGRAGQAPAD VRRETA

References

[1]

"Complete sequence of chromosome 1 of Arthrobacter sp. FB24." 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., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000454 Genomic DNA. Translation: ABK04152.1. Different initiation.
RefSeq	YP_832252.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4444572.
GenomeReviews	Gene locus Arth_2773 in contig CP000454_GR.
KEGG	art:Arth_2773.
TIGR	Arth_2773.
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]
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_ARTS2

Accession

Primary (citable) accession number: A0JYN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 20, 2008
Last modified:	June 16, 2009
This is version 26 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)