Reviewed, UniProtKB/Swiss-Prot A8MAH6 (HEM1_CALMQ)

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:	Cmaq_1730

Organism

Caldivirga maquilingensis (strain DSMZ 13496 / IC-167) [Complete proteome] [HAMAP]

Taxonomic identifier

397948 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Caldivirga

Protein attributes

Sequence length	406 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.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
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 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 – 406	406	Glutamyl-tRNA reductase		PRO_0000335085
Regions
	Nucleotide binding	180 – 185	6	NADP By similarity
	Region	51 – 54	4	Substrate binding By similarity
	Region	106 – 108	3	Substrate binding By similarity
Sites
	Active site	52	1	Nucleophile By similarity
	Binding site	101	1	Substrate By similarity
	Binding site	112	1	Substrate By similarity
	Site	91	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8MAH6-1 [UniParc]. Last modified December 4, 2007. Version 1. Checksum: B5047CF7B54810EA	FASTA	406	45,009
	10 20 30 40 50 60 MGIDDYLSKI RALTLNHKRV STITLSETYF NRDEVYGKLM NYYDEVFLLQ TCNRVEVYVY 70 80 90 100 110 120 GDDDSVAEDM YKVKGTINHV DKLVGMNAVR HIFRVAAGLE SAAVGESEIL GQVEDAFNDA 130 140 150 160 170 180 RKRGALGGLL GFTIERAIRT GKEIRSRFPE ISIGLASIGS LVAEYVHRVR GLNSRIAVIG 190 200 210 220 230 240 AGSIGSDIVR RLAEKGFRNV IIVNRTLDKA KAAALRYGFN YAPIDSLRSV IRDSDVVIFA 250 260 270 280 290 300 TSATNPLLRR RDAEELSGKP IIIDVGVPRN VDPEIPGVVS IDELKNIENE IREGKRKALD 310 320 330 340 350 360 EASRLIELRL IEYRRLFARR VIEGMIGELT KWGLSIGESE VKRAVKAGLI KNEEDGAALA 370 380 390 400 VKSTVKKIML PLLTYLKELA EEDKFDEALI IISGIKAKLN GDGKQS

References

[1]

"Complete sequence of Caldivirga maquilingensis IC-167." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. , Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M., Saltikov C., House C.H., Richardson P. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000852 Genomic DNA. Translation: ABW02553.1.
RefSeq	YP_001541543.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5710155.
GenomeReviews	Gene locus Cmaq_1730 in contig CP000852_GR.
KEGG	cma:Cmaq_1730.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_00087. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd. IPR003462. ODC_Mu_crystall. IPR006151. Shikm_DHase/Glu-tRNA_Rdtase. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR13812. ODC_Mu_crystall. 1 hit.
Pfam	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_CALMQ

Accession

Primary (citable) accession number: A8MAH6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	December 4, 2007
Last modified:	November 25, 2008
This is version 11 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)