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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

Pathwayi: 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.

Pathwayi: 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 lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeThermosynechococcus
Proteomesi
  • UP000000440 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001204601 – 437Glutamate-1-semialdehyde 2,1-aminomutaseAdd BLAST437

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei277N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PRIDEiQ8DLK8.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi197221.tlr0479.

Structurei

Secondary structure

1437
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi48 – 53Combined sources6
Beta strandi55 – 58Combined sources4
Beta strandi63 – 68Combined sources6
Turni69 – 73Combined sources5
Helixi81 – 91Combined sources11
Helixi102 – 114Combined sources13
Beta strandi119 – 126Combined sources8
Helixi127 – 142Combined sources16
Beta strandi146 – 151Combined sources6
Beta strandi188 – 192Combined sources5
Helixi196 – 205Combined sources10
Turni207 – 209Combined sources3
Beta strandi210 – 215Combined sources6
Beta strandi217 – 219Combined sources3
Beta strandi221 – 223Combined sources3
Helixi231 – 241Combined sources11
Beta strandi245 – 250Combined sources6
Turni251 – 256Combined sources6
Helixi261 – 266Combined sources6
Beta strandi271 – 275Combined sources5
Helixi277 – 280Combined sources4
Beta strandi286 – 290Combined sources5
Helixi292 – 295Combined sources4
Helixi314 – 327Combined sources14
Helixi332 – 352Combined sources21
Turni353 – 355Combined sources3
Beta strandi359 – 363Combined sources5
Beta strandi366 – 373Combined sources8
Helixi379 – 382Combined sources4
Helixi387 – 399Combined sources13
Helixi420 – 434Combined sources15

3D structure databases

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

eggNOGiENOG4105CDM. Bacteria.
COG0001. LUCA.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiPOG091H04O1.

Family and domain databases

CDDicd00610. OAT_like. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3. 1 hit.
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 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CFBX-ray2.85A27-437[»]
ProteinModelPortaliQ8DLK8.
SMRiQ8DLK8.
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

eggNOGiENOG4105CDM. Bacteria.
COG0001. LUCA.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiPOG091H04O1.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
UPA00668.

Miscellaneous databases

EvolutionaryTraceiQ8DLK8.

Family and domain databases

CDDicd00610. OAT_like. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3. 1 hit.
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...

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: November 2, 2016
This is version 95 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

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 one 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.