Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P16618 (HEM1_BACSU)

Last modified June 16, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA reductase
      Short name=GluTR
    EC=1.2.1.70
Gene names
Name: hemA
Ordered Locus Names: BSU28170
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

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

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.

Sequence similarities

Belongs to the glutamyl-tRNA reductase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 455455Glutamyl-tRNA reductase HAMAP MF_00087
PRO_0000113996

Regions

Nucleotide binding189 – 1946NADP By similarity
Region49 – 524Substrate binding By similarity
Region114 – 1163Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1091Substrate By similarity
Binding site1201Substrate By similarity
Site991Important for activity By similarity

Experimental info

Mutagenesis1051C → Y: Loss of activity. HAMAP MF_00087

Sequences

Sequence LengthMass (Da)Tools
P16618-1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: B7AD817A5244A629

FASTA45550,844
        10         20         30         40         50         60 
MHILVVGVDY KSAPIEIREK VSFQPNELAE AMVQLKEEKS ILENIIVSTC NRTEIYAVVD 

        70         80         90        100        110        120 
QLHTGRYYIK KFLADWFQLS KEELSPFLTF YESDAAVEHL FRVACGLDSM VIGETQILGQ 

       130        140        150        160        170        180 
VRDSFKTAQQ EKTIGTIFNE LFKQAVTVGK RTHAETDIGS NAVSVSYAAV ELAKKIFGNL 

       190        200        210        220        230        240 
SSKHILILGA GKMGELAAEN LHGQGIGKVT VINRTYLKAK ELADRFSGEA RSLNQLESAL 

       250        260        270        280        290        300 
AEADILISST GASEFVVSKE MMENANKLRK GRPLFMVDIA VPRDLDPALN DLEGVFLYDI 

       310        320        330        340        350        360 
DDLEGIVEAN MKERRETAEK VELLIEETIV EFKQWMNTLG VVPVISALRE KALAIQSETM 

       370        380        390        400        410        420 
DSIERKLPHL STREKKLLNK HTKSIINQML RDPILKVKEL AADADSEEKL ALFMQIFDIE 

       430        440        450 
EAAGRQMMKT VESSQKVHSF KKAESKAGFS PLVSE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the hemA region of the Bacillus subtilis chromosome."
Petricek M., Rutberg L., Schroeder I., Hederstedt L.
J. Bacteriol. 172:2250-2258(1990) [PubMed: 2110138] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism."
Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., Emmerson P.T., Harwood C.R.
Microbiology 142:3067-3078(1996) [PubMed: 8969504] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

M57676 Genomic DNA. Translation: AAA22510.1.
Z75208 Genomic DNA. Translation: CAA99543.1.
AL009126 Genomic DNA. Translation: CAB14777.1.
PIRA35252.
RefSeqNP_390695.1.

3D structure databases

HSSPHSSP built from PDB template 1GPJ based on UniProtKB Q9UXR8.
ModBaseSearch...

Genome annotation databases

GeneID937443.
GenomeReviewsGene locus BSU28170 in contig AL009126_GR.
KEGGbsu:BSU28170.
NMPDRfig|224308.1.peg.2820.

Organism-specific databases

SubtiListBG10340. hemA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP16618.
OMAP16618. GPILNRL.

Enzyme and pathway databases

BioCycBSUB224308:BSU2813-MON.
BRENDA1.2.1.70. 150.

Family and domain databases

HAMAPMF_00087.
[Tree]
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_C.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR003462. ODC_Mu_crystall.
IPR018214. pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR13812. ODC_Mu_crystall. 1 hit.
PfamPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_BACSU
AccessionPrimary (citable) accession number: P16618
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 16, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents