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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

GO - Molecular functioni

  1. glutamate-1-semialdehyde 2,1-aminomutase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: InterPro
  3. transaminase activity Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-965-MONOMER.
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
ProteomesiUP000000532 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000243636Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei266 – 2661N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi300852.TTHA0934.

Structurei

Secondary structure

1
424
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1613Combined sources
Helixi18 – 203Combined sources
Beta strandi21 – 233Combined sources
Helixi24 – 274Combined sources
Turni29 – 313Combined sources
Beta strandi38 – 436Combined sources
Beta strandi45 – 484Combined sources
Beta strandi53 – 586Combined sources
Helixi59 – 613Combined sources
Helixi71 – 8212Combined sources
Helixi92 – 10413Combined sources
Beta strandi110 – 1167Combined sources
Helixi117 – 13216Combined sources
Beta strandi136 – 1405Combined sources
Helixi149 – 1513Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi164 – 1674Combined sources
Helixi172 – 1754Combined sources
Beta strandi178 – 1814Combined sources
Helixi186 – 19611Combined sources
Helixi197 – 1993Combined sources
Beta strandi200 – 2056Combined sources
Beta strandi207 – 2093Combined sources
Helixi219 – 2279Combined sources
Helixi228 – 2314Combined sources
Beta strandi234 – 2385Combined sources
Turni240 – 2456Combined sources
Helixi250 – 2556Combined sources
Beta strandi260 – 2645Combined sources
Helixi266 – 2694Combined sources
Beta strandi275 – 2795Combined sources
Helixi281 – 2844Combined sources
Turni288 – 2903Combined sources
Beta strandi291 – 2933Combined sources
Helixi303 – 31816Combined sources
Helixi321 – 34323Combined sources
Beta strandi349 – 3535Combined sources
Beta strandi356 – 3649Combined sources
Helixi369 – 3724Combined sources
Helixi377 – 38812Combined sources
Turni389 – 3913Combined sources
Beta strandi396 – 4005Combined sources
Helixi410 – 42314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E7UX-ray1.90A1-424[»]
ProteinModelPortaliQ5SJS4.
SMRiQ5SJS4. Positions 1-424.
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

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.
PhylomeDBiQ5SJS4.

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.

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 20, 2004 - v1
Checksum:i8134C11065EEFF77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70757.1.
RefSeqiYP_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.
RefSeqiYP_144200.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E7UX-ray1.90A1-424[»]
ProteinModelPortaliQ5SJS4.
SMRiQ5SJS4. Positions 1-424.
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

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.
PhylomeDBiQ5SJS4.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciTTHE300852:GH8R-965-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SJS4.

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. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.

Entry informationi

Entry nameiGSA_THET8
AccessioniPrimary (citable) accession number: Q5SJS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2006
Last sequence update: December 20, 2004
Last modified: March 31, 2015
This is version 77 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

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.