Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A6VND5

- HEM1_ACTSZ

UniProt

A6VND5 - HEM1_ACTSZ

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Actinobacillus succinogenes (strain ATCC 55618 / 130Z)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501NucleophileUniRule annotation
Sitei104 – 1041Important for activityUniRule annotation
Binding sitei114 – 1141SubstrateUniRule annotation
Binding sitei125 – 1251SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi204 – 2096NADPUniRule annotation

GO - Molecular functioni

  1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciASUC339671:GHDX-1180-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Ordered Locus Names:Asuc_1116
OrganismiActinobacillus succinogenes (strain ATCC 55618 / 130Z)
Taxonomic identifieri339671 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus
ProteomesiUP000001114: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 435435Glutamyl-tRNA reductasePRO_1000071245Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi339671.Asuc_1116.

Structurei

3D structure databases

ProteinModelPortaliA6VND5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni119 – 1213Substrate bindingUniRule annotation

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109650.
KOiK02492.
OMAiLAHKLTN.
OrthoDBiEOG6MWNBM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A6VND5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTILVLGINH KTATVALREK VAFSEEKRLS ALNQIEQLKL AQSTVILSTC
60 70 80 90 100
NRTEVYLHNK FIQPEQNSAW IDECVAWFAA IHQIQLTDLQ DCLYFYQNQQ
110 120 130 140 150
AVTHLMRVAC GLDSLILGEP QILGQVKQAY QLAEEYYQRA HGLGKSAVIS
160 170 180 190 200
SELSRLFQKT FSTAKRVRTE TNIGESAVSV AYAACSLGRQ IFESLQELTI
210 220 230 240 250
LLVGAGETIE LAARHLLRHG VKKLMIANRT RARAEALVAK LESPFIEILS
260 270 280 290 300
LSELQDGLNQ ADIVISSTGS PTTLISYEMM KQAQIQRRYR PVLIVDIAVP
310 320 330 340 350
RDVEESIVKL DSVYHYTVDD LQNIINHNLS EREKASEQAE EIIAEECAAF
360 370 380 390 400
FEWLKVRQAS NLIRTYRESA DEIRQELLEK AQFSLSQGES ADKILDEFST
410 420 430
KLMNKLLHSP TLVMQTMVKQ GDSRGLQNFL SVIKK
Length:435
Mass (Da):49,073
Last modified:August 21, 2007 - v1
Checksum:iF6A876382802D60B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000746 Genomic DNA. Translation: ABR74482.1.
RefSeqiYP_001344417.1. NC_009655.1.

Genome annotation databases

EnsemblBacteriaiABR74482; ABR74482; Asuc_1116.
GeneIDi5348066.
KEGGiasu:Asuc_1116.
PATRICi20760606. VBIActSuc117883_1182.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000746 Genomic DNA. Translation: ABR74482.1 .
RefSeqi YP_001344417.1. NC_009655.1.

3D structure databases

ProteinModelPortali A6VND5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 339671.Asuc_1116.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABR74482 ; ABR74482 ; Asuc_1116 .
GeneIDi 5348066.
KEGGi asu:Asuc_1116.
PATRICi 20760606. VBIActSuc117883_1182.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci ASUC339671:GHDX-1180-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "A genomic perspective on the potential of Actinobacillus succinogenes for industrial succinate production."
    McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A., Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L., Burkhart K.B., Harkins V., Vieille C.
    BMC Genomics 11:680-680(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 55618 / 130Z.

Entry informationi

Entry nameiHEM1_ACTSZ
AccessioniPrimary (citable) accession number: A6VND5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 2007
Last modified: October 1, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3