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Q97MU6

- HEM1_CLOAB

UniProt

Q97MU6 - HEM1_CLOAB

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
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 sitei46 – 461NucleophileUniRule annotation
Sitei91 – 911Important for activityUniRule annotation
Binding sitei101 – 1011SubstrateUniRule annotation
Binding sitei112 – 1121SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi177 – 1826NADPUniRule 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

BioCyciCACE272562:GJIH-104-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:CA_C0095
OrganismiClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Taxonomic identifieri272562 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000000814: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396Glutamyl-tRNA reductasePRO_0000114011Add
BLAST

Proteomic databases

PRIDEiQ97MU6.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272562.CA_C0095.

Structurei

3D structure databases

ProteinModelPortaliQ97MU6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate bindingUniRule annotation
Regioni106 – 1083Substrate 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.
HOGENOMiHOG000090159.
KOiK02492.
OMAiCINDENC.
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.
SUPFAMiSSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q97MU6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIQLLALKRD LKVEIREKFS IIEKRIGDKD VLLKEVCNEV VILSTCNRIE
60 70 80 90 100
IYFNSEKNRK QIIEEIFSKM GWNINFLENF FYCKGDEAIN HLMEVACGFD
110 120 130 140 150
SLILGEDQIL GQIKAAYDTA LKNKTSGSEL KKLFQLVITC GKEFRSISML
160 170 180 190 200
NRIPVSSASI AVNKARQENL RRFMVFGFGD VGSLVCKYIL SSDFDVLYIV
210 220 230 240 250
VRNKAAVSIK DKRIKVLSFN EKNSYYDDVE CMISCTSAPH PVIWEKELPY
260 270 280 290 300
RKFTIFDLAV PRDVEETVYG RNNIDIYDID QISMIDNNNR KKRKEIMMAN
310 320 330 340 350
RHIMSKYIVE FYDWQKVQEI VPDIIKLKLY GESVNKRRYE TFKNKKATKD
360 370 380 390
NDMLVNMLIK STSNVYINRA IEVLKEEQLK GRGEDCLRIL RRIFQK
Length:396
Mass (Da):46,275
Last modified:October 1, 2001 - v1
Checksum:i7FC88271A99566B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001437 Genomic DNA. Translation: AAK78080.1.
PIRiE96911.
RefSeqiNP_346740.1. NC_003030.1.

Genome annotation databases

EnsemblBacteriaiAAK78080; AAK78080; CA_C0095.
GeneIDi1116278.
KEGGicac:CA_C0095.
PATRICi32034459. VBICloAce74127_0278.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001437 Genomic DNA. Translation: AAK78080.1 .
PIRi E96911.
RefSeqi NP_346740.1. NC_003030.1.

3D structure databases

ProteinModelPortali Q97MU6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272562.CA_C0095.

Proteomic databases

PRIDEi Q97MU6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK78080 ; AAK78080 ; CA_C0095 .
GeneIDi 1116278.
KEGGi cac:CA_C0095.
PATRICi 32034459. VBICloAce74127_0278.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000090159.
KOi K02492.
OMAi CINDENC.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CACE272562:GJIH-104-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 SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Entry informationi

Entry nameiHEM1_CLOAB
AccessioniPrimary (citable) accession number: Q97MU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: October 1, 2001
Last modified: October 1, 2014
This is version 97 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