A1RNE2 (HEM1_SHESW) Reviewed, UniProtKB/Swiss-Prot

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:	Sputw3181_3375

Organism

Shewanella sp. (strain W3-18-1) [Complete proteome] [HAMAP]

Taxonomic identifier

351745 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
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. HAMAP MF_00087
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. HAMAP MF_00087
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. HAMAP MF_00087
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. HAMAP MF_00087
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	porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 416	416	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_1000004695
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)
	A1RNE2 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 91C438981E545C54	FASTA	416	45,487
	10 20 30 40 50 60 MSLVAIGINH KTATVDLREK VAFSPDKIHD AMKSLASRTR SGEAVIVSTC NRTELYCNNG 70 80 90 100 110 120 DEADIIEWLE EYHGLDHKDV APCLYNYHGQ TAVKHLMRVA SGLDSLILGE PQILGQVKQA 130 140 150 160 170 180 FAKAKEAGTV ALTIDRLFQN TFSVAKKVRT ETEIGAAAVS VAFAAVSMAK HIFSSLSTTK 190 200 210 220 230 240 VLLIGAGETI ELVAKHLKDN GVASMVVANR TLERAQGMCE EFGATAITLA QIPDYLPKAD 250 260 270 280 290 300 IVISSTASPL PILGKGMVEK ALKQRRHQPM LLVDIAVPRD IEPEVADLDD AFLYTVDDLH 310 320 330 340 350 360 SIIEQNMASR KEAAEQAELI TEEQSYLFMD WVRSLESVDS IREYRNQSMA IKDELVERAL 370 380 390 400 410 NKLAQGGDTE QVLIELANRL TNKLIHAPTQ ALTAASRQGD LNTLGQLRTA LGLDKN

References

[1]

"Complete sequence of Shewanella sp. W3-18-1." US DOE Joint Genome Institute 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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: W3-18-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000503 Genomic DNA. Translation: ABM26187.1.
RefSeq	YP_964741.1. NC_008750.1.
3D structure databases
ProteinModelPortal	A1RNE2.
ModBase	Search...
Protein-protein interaction databases
STRING	A1RNE2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4659229.
GenomeReviews	Gene locus Sputw3181_3375 in contig CP000503_GR.
KEGG	shw:Sputw3181_3375.
PATRIC	23600628. VBISheSp103602_3531.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0373.
HOGENOM	HBG732626.
OMA	YADIVIS.
ProtClustDB	PRK00045.
Family and domain databases
HAMAP	MF_00087. Glu-tRNA_reductase. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_dimer. 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.
KO	K02492.
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.
SUPFAM	SSF69075. 4pyrrol_synth_GluRdtase_C. 1 hit. SSF69742. GlutR. 1 hit.
TIGRFAMs	TIGR01035. HemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_SHESW

Accession

Primary (citable) accession number: A1RNE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 6, 2007
Last modified:	January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program