Reviewed, UniProtKB/Swiss-Prot A1SI37 (HEM12_NOCSJ)

Names and origin

Protein names

Recommended name:
    Glutamyl-tRNA reductase 2
      Short name=GluTR 2
    EC=1.2.1.70

Gene names

Name:	hemA2
Ordered Locus Names:	Noca_1962

Organism

Nocardioides sp. (strain BAA-499 / JS614) [Complete proteome] [HAMAP]

Taxonomic identifier

196162 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Nocardioidaceae › Nocardioides

Protein attributes

Sequence length	448 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 – 448	448	Glutamyl-tRNA reductase 2 HAMAP MF_00087		PRO_0000335056
Regions
	Nucleotide binding	190 – 195	6	NADP By similarity
	Region	50 – 53	4	Substrate binding By similarity
	Region	114 – 116	3	Substrate binding By similarity
Sites
	Active site	51	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

Sequences

	Sequence		Length	Mass (Da)
	A1SI37-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: D6E37EAE8352C2A1	FASTA	448	46,537
	10 20 30 40 50 60 MSRLTCLAFP GRSIPMAVLE RLSVAARELP ASVRALRAVP GVDQVLVLST CERTEVYAWW 70 80 90 100 110 120 TDEADPAALL RALAGQRGLG PEPLLEHAVG LTGREAVQHL LRVTAGLDSF VRGESDIVGQ 130 140 150 160 170 180 VRAAVQAARA EGAVGLEVQR LVDAAVNTSR RVHRSTGAGL AAGSVASTAV AAVAGLLPDG 190 200 210 220 230 240 LAGRDLLVVG TGQVAVSVVA AAREAGARLT VCGRDPERAA AIAPAGARVL GLDDLPGALL 250 260 270 280 290 300 DADAVVFGTS SPERLLRAGD LGPGLSEHRS GRELVVVDLC VPRNVDPDVR GVPGVRLLDL 310 320 330 340 350 360 TDLRGAAVPG RRPSAPAPAA LELAEQIVAQ EVDRFLHWWV DRAAAEPVRR LRADVEACVR 370 380 390 400 410 420 EEVARATRGL SPDLEPLVAE GIRRAVQHLA HGPTRRLLDA AAAGEDEVVA LLAGLFAPSA 430 440 EEDQAVPAYS PQPIGNTSNA AASATPRR

References

[1]

"Complete sequence of chromosome 1 of Nocardioides sp. JS614." 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., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. , Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000509 Genomic DNA. Translation: ABL81472.1.
RefSeq	YP_923159.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4599868.
GenomeReviews	Gene locus Noca_1962 in contig CP000509_GR.
KEGG	nca:Noca_1962.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A1SI37. RAVNEDI.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM12_NOCSJ

Accession

Primary (citable) accession number: A1SI37

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 6, 2007
Last modified:	June 16, 2009
This is version 27 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)