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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathway: protoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Pathway: chlorophyll biosynthesis

This protein is involved in the pathway chlorophyll biosynthesis, which is part of Porphyrin-containing compound metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway chlorophyll biosynthesis and in Porphyrin-containing compound metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
UPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSAUniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferaseUniRule annotation
Short name:
GSA-ATUniRule annotation
Gene namesi
Name:hemLUniRule annotation
Ordered Locus Names:tlr0479
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
ProteomesiUP000000440 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 437437Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120460Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei277 – 2771N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiQ8DLK8.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi197221.tlr0479.

Structurei

Secondary structure

1
437
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi48 – 536Combined sources
Beta strandi55 – 584Combined sources
Beta strandi63 – 686Combined sources
Turni69 – 735Combined sources
Helixi81 – 9111Combined sources
Helixi102 – 11413Combined sources
Beta strandi119 – 1268Combined sources
Helixi127 – 14216Combined sources
Beta strandi146 – 1516Combined sources
Beta strandi188 – 1925Combined sources
Helixi196 – 20510Combined sources
Turni207 – 2093Combined sources
Beta strandi210 – 2156Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi221 – 2233Combined sources
Helixi231 – 24111Combined sources
Beta strandi245 – 2506Combined sources
Turni251 – 2566Combined sources
Helixi261 – 2666Combined sources
Beta strandi271 – 2755Combined sources
Helixi277 – 2804Combined sources
Beta strandi286 – 2905Combined sources
Helixi292 – 2954Combined sources
Helixi314 – 32714Combined sources
Helixi332 – 35221Combined sources
Turni353 – 3553Combined sources
Beta strandi359 – 3635Combined sources
Beta strandi366 – 3738Combined sources
Helixi379 – 3824Combined sources
Helixi387 – 39913Combined sources
Helixi420 – 43415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CFBX-ray2.85A27-437[»]
ProteinModelPortaliQ8DLK8.
SMRiQ8DLK8. Positions 11-437.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8DLK8.

Family & Domainsi

Sequence similaritiesi

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3.
InterProiIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8DLK8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRELTLTTTV FQTTKSQEIF AAAQKLMPGG VSSPVRAFKS VGGQPIVFDH
60 70 80 90 100
VKGAHIWDVD GNQYIDYVGS WGPAIVGHAH PEVIDALHAA LEKGTSFGAP
110 120 130 140 150
CLLENILAEM VIAAVPSVEM VRFVNSGTEA CMAVLRLMRA YTQREKVIKF
160 170 180 190 200
EGCYHGHADM FLVKAGSGVA TLGLPDSPGV PKATTAATLT APYNDLEAVS
210 220 230 240 250
RLFEQYPNDI AGVILEPVVG NAGFIPPDAG FLEGLRELTK QYGALLVFDE
260 270 280 290 300
VMTGFRIAYG GAQEKFGVTP DLTTLGKVIG GGLPVGAYGG RAEIMKMVAP
310 320 330 340 350
AGPVYQAGTL SGNPLAMTAG IKTLEILSRP GSYEHLDRIT GKLVQGLLDA
360 370 380 390 400
AREFGHEVCG GHISGMFGLF FTAGPVTNYE QAKQSDLKKF AAFHRGMLEQ
410 420 430
GIYLAPSQFE AGFTSLAHTE ADIERTIAAA RTVLSQL
Length:437
Mass (Da):46,450
Last modified:June 20, 2003 - v2
Checksum:i5FDD56F62A179C23
GO

Sequence cautioni

The sequence BAC08031.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC08031.1. Different initiation.
RefSeqiNP_681269.2. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC08031; BAC08031; BAC08031.
GeneIDi1012458.
KEGGitel:tlr0479.
PATRICi23926202. VBITheElo119873_0504.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC08031.1. Different initiation.
RefSeqiNP_681269.2. NC_004113.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CFBX-ray2.85A27-437[»]
ProteinModelPortaliQ8DLK8.
SMRiQ8DLK8. Positions 11-437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi197221.tlr0479.

Proteomic databases

PRIDEiQ8DLK8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC08031; BAC08031; BAC08031.
GeneIDi1012458.
KEGGitel:tlr0479.
PATRICi23926202. VBITheElo119873_0504.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
UPA00668.

Miscellaneous databases

EvolutionaryTraceiQ8DLK8.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3.
InterProiIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BP-1.

Entry informationi

Entry nameiGSA_THEEB
AccessioniPrimary (citable) accession number: Q8DLK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: April 1, 2015
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.