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C1F252 (C1F252_ACIC5) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamyl-tRNA reductase HAMAP MF_00087
Short name=GluTR HAMAP MF_00087
EC=1.2.1.70 HAMAP MF_00087
Gene names
Name:hemA HAMAP MF_00087 EMBL ACO31610.1
Ordered Locus Names:ACP_0712
OrganismAcidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670) [Complete proteome] [HAMAP]
Taxonomic identifier240015 [NCBI]
Taxonomic lineageBacteria › Acidobacteria › Acidobacteriales › Acidobacteriaceae › Acidobacterium

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Protein existenceInferred 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 SAAS SAAS018214

Catalytic activity

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214

Subunit structure

Homodimer By similarity. HAMAP MF_00087 SAAS SAAS018214

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding188 – 1936NADP By similarity HAMAP MF_00087
Region49 – 524Substrate binding By similarity HAMAP MF_00087
Region113 – 1153Substrate binding By similarity HAMAP MF_00087

Sites

Active site501Nucleophile By similarity HAMAP MF_00087
Binding site1081Substrate By similarity HAMAP MF_00087
Binding site1191Substrate By similarity HAMAP MF_00087
Site981Important for activity By similarity HAMAP MF_00087

Sequences

Sequence LengthMass (Da)Tools
C1F252 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 3B038A3D47403549

FASTA47751,996
        10         20         30         40         50         60 
MNLLLTGLNH KTAPVELRER LSIPEDALAA VTAQVLALPG VDEAVILSTC NRVELLIAHR 

        70         80         90        100        110        120 
ERVAEPDMAA FLEECFQLSG SGLREHLYHH REAEAVRHLF RVACSLDSLV LGESQILGQV 

       130        140        150        160        170        180 
KAAYAAAKEN GAVRSQLDRL LQETFALAKR VRTETEIGAA PVNISSVAVD LARRIFGSLD 

       190        200        210        220        230        240 
GKRVLLLGAG KMSELAARHL VHHGANRILV ANRTLARAEA LAAQFNGEAI TFDAVFSLQD 

       250        260        270        280        290        300 
VPDILITSTG APRPILTAAH VQQFLHRRRR KPMLLVDIAV PRDVEPEVNR LEGAFLYDID 

       310        320        330        340        350        360 
DLQSVASANL TDRKRQAELA EEIVAAEAIK FEQKRRSLEI GPVISGMQQT VEALCEAELQ 

       370        380        390        400        410        420 
RLAPRMHSMT DEQYAAVKML TRGLMNKFLH LPKQALRSAA QTGDDAAVRA IQSAFDPSVL 

       430        440        450        460        470 
RTGPKGDLAC PRSGVSMDDV KREKARGHHA EQGSTASAPA EAATDSAFSD EIPARRH

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001472 Genomic DNA. Translation: ACO31610.1.
RefSeqYP_002753830.1. NC_012483.1.

3D structure databases

ProteinModelPortalC1F252.
ModBaseSearch...

Protein-protein interaction databases

STRINGC1F252.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7700293.
GenomeReviewsGene locus ACP_0712 in contig CP001472_GR.
KEGGaca:ACP_0712.
PATRIC20664783. VBIAciCap40988_0686.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAGPILNRL.
ProtClustDBCLSK2467658.

Family and domain databases

HAMAPMF_00087. Glu_tRNA_reductase.
[Tree]
InterProIPR000343. 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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK02492.
PfamPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMSSF69075. 4pyrrol_synth_GluRdtase_C. 1 hit.
SSF69742. GlutR. 1 hit.
TIGRFAMsTIGR01035. HemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC1F252_ACIC5
AccessionPrimary (citable) accession number: C1F252
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: December 14, 2011
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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