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B9LKR5

- HEM1_CHLSY

UniProt

B9LKR5 - HEM1_CHLSY

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl)
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 sitei55 – 551NucleophileUniRule annotation
Sitei103 – 1031Important for activityUniRule annotation
Binding sitei113 – 1131SubstrateUniRule annotation
Binding sitei124 – 1241SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi193 – 1986NADPUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciCSP480224:GHIY-2845-MONOMER.
UniPathwayiUPA00251; UER00316.
UPA00668.

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:Chy400_2802
OrganismiChloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl)
Taxonomic identifieri480224 [NCBI]
Taxonomic lineageiBacteriaChloroflexiChloroflexiaChloroflexalesChloroflexineaeChloroflexaceaeChloroflexus
ProteomesiUP000007725: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Glutamyl-tRNA reductasePRO_1000190512Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi480224.Chy400_2802.

Structurei

3D structure databases

ProteinModelPortaliB9LKR5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 574Substrate bindingUniRule annotation
Regioni118 – 1203Substrate 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.
HOGENOMiHOG000109649.
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.
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.

Sequencei

Sequence statusi: Complete.

B9LKR5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNLFLAGLDH TTAPVEIREQ LAFSQTDLPS ALMQLTSSET GTPPLFAEAV
60 70 80 90 100
ILSTCNRVEL YGVTNPGTTA QHVVDFLAAF HRRPAASFVH TLYFYQGEAV
110 120 130 140 150
ARHLCATAAG LRSLVLGEAQ IQGQVRNAYE AAQRIGSVGS ILHRLFQIAL
160 170 180 190 200
VAGKRVRHET TIGKGAASVS QAGVELARRR LGDLRGREVL LIGGGEVSEL
210 220 230 240 250
AAQNLIANGA DRLTIVNRTS ARAAALAERY GAEMLDFGAL PQALARADIV
260 270 280 290 300
ISSTAAPVPI IYRHHVAEAI AHKQRARACG ECDPPTMLLI DLAVPRDIAA
310 320 330 340 350
DVAQIPGVHL FTVDDLREVV SHTIELRSAV LEIAQQIVEE QVQEFLSWMR
360 370 380 390 400
TQEALPVLTM LRQRAEEVRN EELARALRRL HDLSPEQRAV IEGLSRSIVN
410 420 430
KLLHPPTRCL REAAAHGQGK RYASILAELF NLEH
Length:434
Mass (Da):47,296
Last modified:March 24, 2009 - v1
Checksum:i1A101A099F18E489
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001364 Genomic DNA. Translation: ACM54190.1.
RefSeqiWP_015909256.1. NC_012032.1.
YP_002570516.1. NC_012032.1.

Genome annotation databases

EnsemblBacteriaiACM54190; ACM54190; Chy400_2802.
GeneIDi7404273.
KEGGichl:Chy400_2802.
PATRICi21425247. VBIChlSp61043_2903.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001364 Genomic DNA. Translation: ACM54190.1 .
RefSeqi WP_015909256.1. NC_012032.1.
YP_002570516.1. NC_012032.1.

3D structure databases

ProteinModelPortali B9LKR5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 480224.Chy400_2802.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACM54190 ; ACM54190 ; Chy400_2802 .
GeneIDi 7404273.
KEGGi chl:Chy400_2802.
PATRICi 21425247. VBIChlSp61043_2903.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109649.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
UPA00668 .
BioCyci CSP480224:GHIY-2845-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.
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.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29364 / DSM 637 / Y-400-fl.

Entry informationi

Entry nameiHEM1_CHLSY
AccessioniPrimary (citable) accession number: B9LKR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: October 1, 2014
This is version 44 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

Documents

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

External Data

Dasty 3