A1SV88 (HEM1_PSYIN) 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:	Ping_1606

Organism

Psychromonas ingrahamii (strain 37) [Complete proteome] [HAMAP]

Taxonomic identifier

357804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Psychromonadaceae › Psychromonas › Psychromonas ingrahamii

Protein attributes

Sequence length	419 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-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP-Rule MF_00087
Subunit structure	Homodimer By similarity. HAMAP-Rule 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-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.
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	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: UniProtKB-HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 419	419	Glutamyl-tRNA reductase HAMAP-Rule MF_00087		PRO_1000004678
Regions
	Nucleotide binding	187 – 192	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	112 – 114	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	107	1	Substrate By similarity
	Binding site	118	1	Substrate By similarity
	Site	97	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1SV88 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: AD814071E15F5CFB	FASTA	419	46,623
	10 20 30 40 50 60 MPLFALGINH QTASVALREK VAFSADLLLD AYQALLAQPT VLEAVIVSTC NRTEIYCHLK 70 80 90 100 110 120 QDNCDEVIKW LCSFHQIEDH KLRPSLYCYS EYQAIQHLFR VSCGLDSLVL GEPQILGQIK 130 140 150 160 170 180 QAFATAKQAK GVDKIVQKWF QHTFTVAKRV RTETQIGANA ISVAFAAVCL AKQIFSDLSQ 190 200 210 220 230 240 SRVLLIGAGE TIELVGKYLI EHQVPNITIA NRTLSRAMAL VEQFDAQAIT LGEIPNHLAQ 250 260 270 280 290 300 ADIIISSTAS PLPIIGKGMV ERALKARRNR PMLFIDIAVP RDIEAEVSEL RDIYLYSVDD 310 320 330 340 350 360 LQGIIEENKQ ARQVAALEAE KIIDGCIVDF ISWIESLKAV ESIRTYRQNS EQLRDDLLNR 370 380 390 400 410 ASAALQNGEE AENVLKELAF KLTNKLIHHP SLALNETARS GNDDELILLR NALGLSKKD

References

[1]

"Complete sequence of Psychromonas ingrahamii 37." 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., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. , Land M., Hauser L., Kyrpides N., Ivanova N., Staley J., Richardson P. Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 37.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000510 Genomic DNA. Translation: ABM03403.1.
RefSeq	YP_943002.1. NC_008709.1.
3D structure databases
ProteinModelPortal	A1SV88.
ModBase	Search...
Protein-protein interaction databases
STRING	357804.Ping_1606.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABM03403; ABM03403; Ping_1606.
GeneID	4624635.
KEGG	pin:Ping_1606.
PATRIC	23068299. VBIPsyIng103130_1759.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0373.
HOGENOM	HOG000109650.
KO	K02492.
OMA	RTEIYCA.
OrthoDB	EOG6MWNBM.
Enzyme and pathway databases
BioCyc	PING357804:GJBJ-1683-MONOMER.
UniPathway	UPA00251; UER00316.
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. IPR018214. Pyrrol_synth_GluRdtase_CS. 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. SSF69075. 1 hit. SSF69742. SSF69742. 1 hit.
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_PSYIN

Accession

Primary (citable) accession number: A1SV88

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 6, 2007
Last modified:	November 13, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program