Glutamyl-tRNA reductase - Neisseria meningitidis serogroup C

Preferred order of sections

Names and origin

Protein names

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

Gene names

Name:

hemA

Organism

Neisseria meningitidis serogroup C

Taxonomic identifier

135720 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria ›

Protein attributes

Sequence length	415 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
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	Porphyrin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 415

415

Glutamyl-tRNA reductase HAMAP-Rule MF_00087

PRO_0000114047

Regions

Nucleotide binding

184 – 189

6

NADP By similarity

Region

49 – 52

4

Substrate binding By similarity

Region

109 – 111

3

Substrate binding By similarity

Sites

Active site

50

1

Nucleophile By similarity

Binding site

104

1

Substrate By similarity

Binding site

115

1

Substrate By similarity

Site

94

1

Important for activity By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0A0T8 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: C17639CBD6791ECB
Show »

FASTA

415

45,472

        10         20         30         40         50         60 
MQLTAVGLNH QTAPLSIREK LAFAAACLPE AVRNLARSNA ATEAVILSTC NRTELYCVGD 

        70         80         90        100        110        120 
SEEIIRWLAD YHSLPIEEIS PYLYTLGMQE TVRHAFRVAC GLDSMVLGEP QILGQIKDAV 

       130        140        150        160        170        180 
RVAQEQESMG KKLNALFQKT FSVAKEVRTD TAVGENSVSM ASASVKLAEQ IFPDIGDLNV 

       190        200        210        220        230        240 
LFIGAGEMIE LVATYFAAKS PRLMTVANRT LARAQELCDK LGVNAEPCLL SDLPAILHEY 

       250        260        270        280        290        300 
DVVVSSTASQ LPIVGKGMVE RALKQRQSMP LFMLDLAVPR DIEAEVGDLN DAYLYTVDDM 

       310        320        330        340        350        360 
VNIVQSGKEA RQKAAAAAET LVSEKVAEFV RQQQGRQSVP LIRALRDEGE KARKQVLENA 

       370        380        390        400        410 
MKQLAKGATA EEVLERLSIQ LTNKLLHSPT QTLNKAGEED KDLVHAVAQI YHLDK

« Hide

References

[1]

"Transport of intact porphyrin by HpuAB, the hemoglobin-haptoglobin utilization system of Neisseria meningitidis."
Lewis L.A., Sung M., Gipson M., Hartman K., Dyer D.W.
J. Bacteriol. 180:6043-6047(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DNM2 / Serogroup C / Serotype 2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF067427 Genomic DNA. Translation: AAC79429.1.
3D structure databases
ProteinModelPortal	P0A0T8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
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. 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_NEIMC

Accession

Primary (citable) accession number: P0A0T8
Secondary accession number(s): Q9ZHD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	April 3, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families