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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.

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:TTHA0934
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 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_00002436361 – 424Glutamate-1-semialdehyde 2,1-aminomutaseAdd BLAST424

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei266N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi300852.TTHA0934.

Structurei

Secondary structure

1424
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 16Combined sources13
Helixi18 – 20Combined sources3
Beta strandi21 – 23Combined sources3
Helixi24 – 27Combined sources4
Turni29 – 31Combined sources3
Beta strandi38 – 43Combined sources6
Beta strandi45 – 48Combined sources4
Beta strandi53 – 58Combined sources6
Helixi59 – 61Combined sources3
Helixi71 – 82Combined sources12
Helixi92 – 104Combined sources13
Beta strandi110 – 116Combined sources7
Helixi117 – 132Combined sources16
Beta strandi136 – 140Combined sources5
Helixi149 – 151Combined sources3
Beta strandi152 – 154Combined sources3
Beta strandi157 – 159Combined sources3
Beta strandi164 – 167Combined sources4
Helixi172 – 175Combined sources4
Beta strandi178 – 181Combined sources4
Helixi186 – 196Combined sources11
Helixi197 – 199Combined sources3
Beta strandi200 – 205Combined sources6
Beta strandi207 – 209Combined sources3
Helixi219 – 227Combined sources9
Helixi228 – 231Combined sources4
Beta strandi234 – 238Combined sources5
Turni240 – 245Combined sources6
Helixi250 – 255Combined sources6
Beta strandi260 – 264Combined sources5
Helixi266 – 269Combined sources4
Beta strandi275 – 279Combined sources5
Helixi281 – 284Combined sources4
Turni288 – 290Combined sources3
Beta strandi291 – 293Combined sources3
Helixi303 – 318Combined sources16
Helixi321 – 343Combined sources23
Beta strandi349 – 353Combined sources5
Beta strandi356 – 364Combined sources9
Helixi369 – 372Combined sources4
Helixi377 – 388Combined sources12
Turni389 – 391Combined sources3
Beta strandi396 – 400Combined sources5
Helixi410 – 423Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E7UX-ray1.90A1-424[»]
ProteinModelPortaliQ5SJS4.
SMRiQ5SJS4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SJS4.

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.
PhylomeDBiQ5SJS4.

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.

Q5SJS4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERPISEAYF QEAKRHIPGG VSSPVRAFKA VGGTPPFLVR GEGAYVWDAD
60 70 80 90 100
GNRYLDYVMS WGPLILGHAH PKVLARVRET LERGLTFGAP SPLEVALAKK
110 120 130 140 150
VKRAYPFVDL VRFVNSGTEA TMSALRLARG YTGRPYIVKF RGNYHGHADG
160 170 180 190 200
LLVEAGSGAL TLGVPSSAGV PEEYAKLTLV LEYNDPEGLR EVLKRRGEEI
210 220 230 240 250
AAIIFEPVVG NAGVLVPTED FLKALHEAKA YGVLLIADEV MTGFRLAFGG
260 270 280 290 300
ATELLGLKPD LVTLGKILGG GLPAAAYAGR REIMEKVAPL GPVYQAGTLS
310 320 330 340 350
GNPLAMAAGL ATLELLEENP GYYAYLEDLG ARLEAGLKEV LKEKGLPHTV
360 370 380 390 400
NRVGSMITVF FTEGPVVTFQ DARRTDTELF KRFFHGLLDR GIYWPPSNFE
410 420
AAFLSVAHRE EDVEKTLEAL RKAL
Length:424
Mass (Da):46,034
Last modified:December 21, 2004 - v1
Checksum:i8134C11065EEFF77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70757.1.
RefSeqiWP_011228305.1. NC_006461.1.
YP_144200.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70757; BAD70757; BAD70757.
GeneIDi3168378.
KEGGittj:TTHA0934.
PATRICi23956832. VBITheThe93045_0917.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70757.1.
RefSeqiWP_011228305.1. NC_006461.1.
YP_144200.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E7UX-ray1.90A1-424[»]
ProteinModelPortaliQ5SJS4.
SMRiQ5SJS4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0934.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70757; BAD70757; BAD70757.
GeneIDi3168378.
KEGGittj:TTHA0934.
PATRICi23956832. VBITheThe93045_0917.

Phylogenomic databases

eggNOGiENOG4105CDM. Bacteria.
COG0001. LUCA.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
PhylomeDBiQ5SJS4.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.

Miscellaneous databases

EvolutionaryTraceiQ5SJS4.

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_THET8
AccessioniPrimary (citable) accession number: Q5SJS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 84 of the entry and version 1 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.