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Protein

Glutamate-1-semialdehyde 2,1-aminomutase 1

Gene

hemL1

Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
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

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

BioCyciLMON169963:LMO1553-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:lmo1553
OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Taxonomic identifieri169963 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
Proteomesi
  • UP000000817 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 – 429429Glutamate-1-semialdehyde 2,1-aminomutase 1PRO_0000120419Add
BLAST

Amino acid modifications

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

Proteomic databases

PaxDbiQ8Y6X8.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

GO - Molecular functioni

Protein-protein interaction databases

STRINGi169963.lmo1553.

Structurei

3D structure databases

ProteinModelPortaliQ8Y6X8.
SMRiQ8Y6X8. Positions 36-425.
ModBaseiSearch...
MobiDBiSearch...

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.
OrthoDBiEOG6QVRHN.
PhylomeDBiQ8Y6X8.

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.

Q8Y6X8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQNYSKSEKA FKEAKKVLPG GVNSPVRAFN SVDASPVFMD HGKGAYITDV
60 70 80 90 100
DGNEYIDYVL SWGPLILGHT DPAVVNAITK AALKGTSFGT PTEIETELAK
110 120 130 140 150
LVIERVPSIE IVRMVSSGTE ATMSAIRLAR GYTKREKILK FEGSYHGHGD
160 170 180 190 200
SLLIKAGSGV ATLGLPDSPG VTKGLAADTI TVPYNDIEGA KLAFEKYGEE
210 220 230 240 250
IAAVIVEPVA GNMGVVPPIE GFLEGLRELT TKFGSLLIFD EVMTGFRVDY
260 270 280 290 300
YSAQGYYVVT PDLTCLGKVI GGGLPVGAYG GKKEIMEQIA PAGSIYQAGT
310 320 330 340 350
LSGNPLAMNA GFETVRQLTP QHYDVFRTLI KRMEEGLTEI SARRQVPLSI
360 370 380 390 400
NKAGSMFGFF FTDQKVINFD TAKTSNLEFF RNYYREMLGQ GIFLPPSQFE
410 420
GVFISTMHTE NEIDKTLEAF DTTCKILRG
Length:429
Mass (Da):46,603
Last modified:March 1, 2002 - v1
Checksum:i3CEBE0CB96658E9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591979 Genomic DNA. Translation: CAC99631.1.
PIRiAI1268.
RefSeqiNP_465078.1. NC_003210.1.
WP_009931591.1. NC_003210.1.

Genome annotation databases

EnsemblBacteriaiCAC99631; CAC99631; CAC99631.
GeneIDi986918.
KEGGilmo:lmo1553.
PATRICi20312235. VBILisMon69206_1594.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591979 Genomic DNA. Translation: CAC99631.1.
PIRiAI1268.
RefSeqiNP_465078.1. NC_003210.1.
WP_009931591.1. NC_003210.1.

3D structure databases

ProteinModelPortaliQ8Y6X8.
SMRiQ8Y6X8. Positions 36-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi169963.lmo1553.

Proteomic databases

PaxDbiQ8Y6X8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC99631; CAC99631; CAC99631.
GeneIDi986918.
KEGGilmo:lmo1553.
PATRICi20312235. VBILisMon69206_1594.

Phylogenomic databases

eggNOGiENOG4105CDM. Bacteria.
COG0001. LUCA.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.
PhylomeDBiQ8Y6X8.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciLMON169963:LMO1553-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-679 / EGD-e.

Entry informationi

Entry nameiGSA1_LISMO
AccessioniPrimary (citable) accession number: Q8Y6X8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: March 1, 2002
Last modified: February 17, 2016
This is version 91 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

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.