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A1U368

- HEM1_MARAV

UniProt

A1U368 - HEM1_MARAV

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Protein

Glutamyl-tRNA reductase

Gene
hemA, Maqu_2361
Organism
Marinobacter aquaeolei (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter hydrocarbonoclasticus (strain DSM 11845))
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) By similarity.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 – 501Nucleophile By similarity
Sitei97 – 971Important for activity By similarity
Binding sitei107 – 1071Substrate By similarity
Binding sitei118 – 1181Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi187 – 1926NADP By similarity

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

BioCyciMHYD351348:GHYZ-2409-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:Maqu_2361
OrganismiMarinobacter aquaeolei (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter hydrocarbonoclasticus (strain DSM 11845))
Taxonomic identifieri351348 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeMarinobacter
ProteomesiUP000000998: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Glutamyl-tRNA reductaseUniRule annotationPRO_1000004634Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi351348.Maqu_2361.

Structurei

3D structure databases

ProteinModelPortaliA1U368.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni112 – 1143Substrate binding By similarity

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 By similarity.UniRule annotation

Sequence similaritiesi

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.

A1U368-1 [UniParc]FASTAAdd to Basket

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MALVTLGINH RTAPVEIRER VAFTPERMAE AFSELRAASG ASEAAILSTC    50
NRTELYLAGD DDCAPSVLRW LAGFHELDVA DLENVLYVHR DSDAVRHMMR 100
VAAGLDSMVL GEPQILGQLK DAYALAREHS ATGSFLSRLF EQTFSVAKRV 150
RTQTAIGENP VSVAYASVSM AHHIFADMSR NKALLIGAGK TIELVARHLA 200
EAGVRSFLVA NRTLEKAQAL AEAHGGKGIL LSEIPDHLSD VDIVISSTAS 250
PLPILGKGAV ERALKKRKHR PYFMVDIAVP RDIEPEVASL ADVYLYTVDD 300
LRQVIEENIR SREGAAREAE NLISSGVQDF LDQLRALDAV STLKVFRQRA 350
ELLRDVETEK ALRALRNGTD PETALRSLAR GLTNKLLHQP SVQVRKAMAE 400
GRTEVTECLR ELYQLDALEA DEPTTTEKL 429
Length:429
Mass (Da):47,134
Last modified:February 6, 2007 - v1
Checksum:i03E8C1B6367BCF94
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000514 Genomic DNA. Translation: ABM19437.1.
RefSeqiWP_011785824.1. NC_008740.1.
YP_959624.1. NC_008740.1.

Genome annotation databases

EnsemblBacteriaiABM19437; ABM19437; Maqu_2361.
GeneIDi4656425.
KEGGimaq:Maqu_2361.
PATRICi22460048. VBIMarAqu65105_2776.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000514 Genomic DNA. Translation: ABM19437.1 .
RefSeqi WP_011785824.1. NC_008740.1.
YP_959624.1. NC_008740.1.

3D structure databases

ProteinModelPortali A1U368.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 351348.Maqu_2361.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM19437 ; ABM19437 ; Maqu_2361 .
GeneIDi 4656425.
KEGGi maq:Maqu_2361.
PATRICi 22460048. VBIMarAqu65105_2776.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MHYD351348:GHYZ-2409-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. "Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8."
    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., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.
    , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Edwards K., Richardson P.
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700491 / DSM 11845 / VT8.

Entry informationi

Entry nameiHEM1_MARAV
AccessioniPrimary (citable) accession number: A1U368
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: September 3, 2014
This is version 59 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 By similarity.

Keywords - Technical termi

Complete proteome

Documents

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

External Data

Dasty 3

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