A9A1Z3 (A9A1Z3_NITMS) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Glutamyl-tRNA reductase 2 HAMAP MF_00087
Short name=GluTR 2 HAMAP MF_00087
EC=1.2.1.70 HAMAP MF_00087

Gene names

Name:	hemA2 HAMAP MF_00087
Ordered Locus Names:	Nmar_0510

Organism

Nitrosopumilus maritimus (strain SCM1)

Taxonomic identifier

436308 [NCBI]

Taxonomic lineage

Archaea › Thaumarchaeota › marine archaeal group 1 › Nitrosopumilales › Nitrosopumilaceae › Nitrosopumilus

Protein attributes

Sequence length	421 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 RuleBase RU000584
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP MF_00087 RuleBase RU000584
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. HAMAP MF_00087 RuleBase RU000584

Ontologies

Keywords
Biological process	Porphyrin biosynthesis HAMAP MF_00087 RuleBase RU000584
Ligand	NADP HAMAP MF_00087 RuleBase RU000584
Molecular function	Oxidoreductase HAMAP MF_00087 RuleBase RU000584 EMBL ABX12406.1
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: HAMAP
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
Regions
	Nucleotide binding	187 – 192	6	NADP By similarity HAMAP MF_00087
	Region	49 – 52	4	Substrate binding By similarity HAMAP MF_00087
	Region	112 – 114	3	Substrate binding By similarity HAMAP MF_00087
Sites
	Active site	50	1	Nucleophile By similarity HAMAP MF_00087
	Binding site	107	1	Substrate By similarity HAMAP MF_00087
	Binding site	118	1	Substrate By similarity HAMAP MF_00087
	Site	97	1	Important for activity By similarity HAMAP MF_00087

Sequences

	Sequence		Length	Mass (Da)
	A9A1Z3 [UniParc]. Last modified January 15, 2008. Version 1. Checksum: 85C0C3D3E95188C4	FASTA	421	47,386
	10 20 30 40 50 60 MSQNIINARV TFRNSPIHIL ERFTIKDIEE AYDQFKKHSG LDECVIIQTC NRIELFGKSK 70 80 90 100 110 120 SQEVDKIKKT WASLAGLEEQ VFDENMEVEE NQNALHHLLK LTSGLDSMVL GEEQILGQIK 130 140 150 160 170 180 NSITSARERK ASGQHLNTLF DKAIRIGTRI RNNSGIGKGG ISVGSMAVKL AEENIDELKT 190 200 210 220 230 240 KKTLLIGTGE VSTLVAKSLQ RRGYAFDVTS RTLSRSETFC ETMGGTPVKF EEILSGFDNY 250 260 270 280 290 300 DVIFVATTAP YFLVTYERIT EAMKDKNKGM MILDLSNPRT VDEKVATIGG IKLMNLDQIA 310 320 330 340 350 360 EMVEKNMNAR LNKVKTVESI INEEVSVLEA SMKRLEAEPL VKDVFKNIES LREKELQKAL 370 380 390 400 410 420 QMLDEKDEKR IKIIDELTKA VVESIVSTPM NNIRKASEQG NPEVVDLASK LFDYKKQEQA D

References

[1]

"Complete sequence of Nitrosopumilus maritimus SCM1." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., 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., Stahl D., Richardson P. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SCM1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000866 Genomic DNA. Translation: ABX12406.1.
RefSeq	YP_001581844.1. NC_010085.1.
3D structure databases
ProteinModelPortal	A9A1Z3.
ModBase	Search...
Protein-protein interaction databases
STRING	A9A1Z3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5773503.
GenomeReviews	Gene locus Nmar_0510 in contig CP000866_GR.
KEGG	nmr:Nmar_0510.
Phylogenomic databases
HOGENOM	HBG732626.
OMA	IRENEIC.
ProtClustDB	CLSK984355.
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

A9A1Z3_NITMS

Accession

Primary (citable) accession number: A9A1Z3

Entry history

Integrated into UniProtKB/TrEMBL:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	December 14, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)