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Protein

Glutamate-1-semialdehyde 2,1-aminomutase 1

Gene

hemL1

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Pathway:iprotoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (gsaB), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (gsaB), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (gsaB), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase 1 (hemL1), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (gsaB), Glutamate-1-semialdehyde 2,1-aminomutase (gsaB), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (gsaB), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (gsaB), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (gsaB), Glutamate-1-semialdehyde 2,1-aminomutase (gsaB), Glutamate-1-semialdehyde 2,1-aminomutase (gsaB)
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-aminomutase 1 (EC:5.4.3.8)
Short name:
GSA 1
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 1
Short name:
GSA-AT 1
Gene namesi
Name:hemL1
Synonyms:hemL
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

Subcellular locationi

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_0000120451Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei267 – 2671N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiP0C1P8.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi93062.SACOL1714.

Structurei

3D structure databases

ProteinModelPortaliP0C1P8.
SMRiP0C1P8. Positions 3-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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.

P0C1P8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYTKSEEAM KVAETLMPGG VNSPVRAFKS VDTPAIFMDH GKGSKIYDID
60 70 80 90 100
GNEYIDYVLS WGPLILGHRD PQVISHLHEA IDKGTSFGAS TLLENKLAQL
110 120 130 140 150
VIDRVPSIEK VRMVSSGTEA TLDTLRLARG YTGRNKIVKF EGCYHGHSDS
160 170 180 190 200
LLIKAGSGVA TLGLPDSPGV PEGIAKNTIT VPYNDLDALK IAFEKFGNDI
210 220 230 240 250
AGVIVEPVAG NMGVVPPIEG FLQGLRDITT EYGALLIFDE VMTGFRVGYH
260 270 280 290 300
CAQGYFGVTP DLTCLGKVIG GGLPVGAFGG KKEIMDHIAP LGNIYQAGTL
310 320 330 340 350
SGNPLAMTSG YETLSQLTPE TYEYFNMLGD ILEDGLKRVF AKHNVPITVN
360 370 380 390 400
RAGSMIGYFL NEGPVTNFEQ ANKSDLKLFA EMYREMAKEG VFLPPSQFEG
410 420
TFLSTAHTKE DIEKTIQAFD TALSRIVK
Length:428
Mass (Da):46,388
Last modified:July 25, 2006 - v1
Checksum:i88F0566FC5A26D49
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18635 Genomic DNA. Translation: CAB60738.1.
RefSeqiWP_001270868.1. NZ_LBCS01000004.1.

Genome annotation databases

GeneIDi23197461.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18635 Genomic DNA. Translation: CAB60738.1.
RefSeqiWP_001270868.1. NZ_LBCS01000004.1.

3D structure databases

ProteinModelPortaliP0C1P8.
SMRiP0C1P8. Positions 3-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL1714.

Proteomic databases

PRIDEiP0C1P8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi23197461.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.

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. "Antibiotic resistance as a stress response: complete sequencing of a large number of chromosomal loci in Staphylococcus aureus strain COL that impact on the expression of resistance to methicillin."
    de Lencastre H., Wu S.-W., Pinho M.G., Ludovice A.M., Filipe S., Gardete S., Sobral R., Gill S.R., Chung M., Tomasz A.
    Microb. Drug Resist. 5:163-175(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: RUSA233.

Entry informationi

Entry nameiGSA1_STAAU
AccessioniPrimary (citable) accession number: P0C1P8
Secondary accession number(s): O34092, Q9RL91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: July 22, 2015
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.