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Protein

Glutamate-1-semialdehyde 2,1-aminomutase 1

Gene

hemL1

Organism
Geobacillus kaustophilus (strain HTA426)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 2 (hemL2), Glutamate-1-semialdehyde 2,1-aminomutase 1 (hemL1)
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

BioCyciGKAU235909:GJO7-522-MONOMER.
UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase 1UniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSA 1UniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 1UniRule annotation
Short name:
GSA-AT 1UniRule annotation
Gene namesi
Name:hemL1UniRule annotation
Ordered Locus Names:GK0471
OrganismiGeobacillus kaustophilus (strain HTA426)
Taxonomic identifieri235909 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
ProteomesiUP000001172 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 – 428428Glutamate-1-semialdehyde 2,1-aminomutase 1PRO_0000243573Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei268 – 2681N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi235909.GK0471.

Structurei

3D structure databases

ProteinModelPortaliQ5L2S4.
SMRiQ5L2S4. Positions 1-424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiFNDIDSY.
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.

Q5L2S4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQWTKSEQLY KEALQHIVGG VNSPSRSYKA VGGGAPVVME RAQGAYFWDV
60 70 80 90 100
DGNKYIDYLA AYGPIIAGHA HPHIAEAIRR AAETGVLYGT PTPHEITFAK
110 120 130 140 150
MLKEAIPSLE KVRFVNSGTE AVMTTIRVAR AYTGRSKIVK FEGCYHGHSD
160 170 180 190 200
LVLVAAGSGP STLGTPDSAG VPPSIAQEVI TVPYNDVESF REAMNVWGEQ
210 220 230 240 250
VAAVLVEPIV GNFGIVLPKP GFLEAINEIA HKEGALVIYD EVITAFRFMY
260 270 280 290 300
GGAQNLLGVE PDLTAMGKII GGGLPIGAYG GRQDIMEQVA PLGPAYQAGT
310 320 330 340 350
MAGNPASVLA GIACLEVLKQ EGVYEHLDRL GAMLEEGILA HARQCGLPVT
360 370 380 390 400
VNRLKGALTV FFTDEKVENY KQAQRSDGEL FAKFFKLMLK QGINLAPSKY
410 420
EAWFITLAHT EDDIAYTIDA VGKAFRQL
Length:428
Mass (Da):46,142
Last modified:February 1, 2005 - v1
Checksum:i0EDA647DF671CD7A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000043 Genomic DNA. Translation: BAD74756.1.
RefSeqiWP_011229975.1. NC_006510.1.
YP_146324.1. NC_006510.1.

Genome annotation databases

EnsemblBacteriaiBAD74756; BAD74756; GK0471.
GeneIDi3184633.
KEGGigka:GK0471.
PATRICi21962111. VBIGeoKau81518_0551.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000043 Genomic DNA. Translation: BAD74756.1.
RefSeqiWP_011229975.1. NC_006510.1.
YP_146324.1. NC_006510.1.

3D structure databases

ProteinModelPortaliQ5L2S4.
SMRiQ5L2S4. Positions 1-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi235909.GK0471.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD74756; BAD74756; GK0471.
GeneIDi3184633.
KEGGigka:GK0471.
PATRICi21962111. VBIGeoKau81518_0551.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiFNDIDSY.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciGKAU235909:GJO7-522-MONOMER.

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. "Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus."
    Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.
    Nucleic Acids Res. 32:6292-6303(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HTA426.

Entry informationi

Entry nameiGSA1_GEOKA
AccessioniPrimary (citable) accession number: Q5L2S4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: February 1, 2005
Last modified: May 27, 2015
This is version 78 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.