A9WIS2 (HEM1_CHLAA) 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:	Caur_2593

Organism

Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl) [Reference proteome] [HAMAP]

Taxonomic identifier

324602 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Chloroflexi › Chloroflexi › Chloroflexales › Chloroflexaceae › Chloroflexus › Chloroflexus aurantiacus

Protein attributes

Sequence length	434 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-Rule MF_00087
Catalytic activity	L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP-Rule MF_00087
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP-Rule MF_00087 Porphyrin biosynthesis; chlorophyll biosynthesis. HAMAP-Rule 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. HAMAP-Rule 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-Rule MF_00087
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 Reference proteome
Gene Ontology (GO)
Biological_process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: HAMAP protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	NADP binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 434	434	Glutamyl-tRNA reductase HAMAP-Rule MF_00087		PRO_1000075402
Regions
	Nucleotide binding	193 – 198	6	NADP By similarity
	Region	54 – 57	4	Substrate binding By similarity
	Region	118 – 120	3	Substrate binding By similarity
Sites
	Active site	55	1	Nucleophile By similarity
	Binding site	113	1	Substrate By similarity
	Binding site	124	1	Substrate By similarity
	Site	103	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9WIS2 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 1A101A099F052555	FASTA	434	47,312
	10 20 30 40 50 60 MNLFLAGLDH TTAPVEIREQ LAFSQTDLPS ALMQLTSSET GTPPLFAEAV ILSTCNRVEL 70 80 90 100 110 120 YGVTNPGTTA QHVVDFLAAF HRRPAASFVH TLYFYQGEAV ARHLCATAAG LRSLVLGEAQ 130 140 150 160 170 180 IQGQVRNAYE AAQRIGSVGS ILHRLFQIAL VAGKRVRHET TIGKGAASVS QAGVELARRR 190 200 210 220 230 240 LGDLRGREVL LIGGGEVSEL AAQNLIANGA DRLTIVNRTS ARAAALAERY GAEMLDFGAL 250 260 270 280 290 300 PQALARADIV ISSTAAPVPI IYRHHVAEAI AHKQRARACG ECDPPTMLLI DLAVPRDIAA 310 320 330 340 350 360 DVAQIPGVHL FTVDDLREVV SHTIELRSAV LEIAQQIVEE QVQEFLSWMR TQEALPVLTM 370 380 390 400 410 420 LRQRAEEVRN EELARALRRL HDLSPEQRAV IEGLSRSIVN KLLHLPTRCL REAAAHGQGK 430 RYASILAELF NLEH

References

[1]

"Complete sequence of Chloroflexus aurantiacus J-10-fl." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Pierson B.K., Blankenship R.E., Richardson P. Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29366 / DSM 635 / J-10-fl.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000909 Genomic DNA. Translation: ABY35799.1.
RefSeq	YP_001636188.1. NC_010175.1.
3D structure databases
ProteinModelPortal	A9WIS2.
ModBase	Search...
Protein-protein interaction databases
STRING	324602.Caur_2593.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABY35799; ABY35799; Caur_2593.
GeneID	5827062.
KEGG	cau:Caur_2593.
PATRIC	21416349. VBIChlAur28763_2921.
Phylogenomic databases
eggNOG	COG0373.
HOGENOM	HOG000109650.
KO	K02492.
OMA	GPILNRL.
ProtClustDB	CLSK2477151.
Enzyme and pathway databases
BioCyc	CAUR324602:GIXU-2637-MONOMER.
UniPathway	UPA00251; UER00316. UPA00668.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_00087. Glu-tRNA_reductase.
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_dimer. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd_dom. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view]
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_CHLAA

Accession

Primary (citable) accession number: A9WIS2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	May 1, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program