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Protein

Glutamate-1-semialdehyde 2,1-aminomutase 2

Gene

hemL2

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

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

BioCyciLMON169963:LMO1685-MONOMER.
UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase 2UniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSA 2UniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 2UniRule annotation
Short name:
GSA-AT 2UniRule annotation
Gene namesi
Name:hemL2UniRule annotation
Synonyms:gsaB
Ordered Locus Names:lmo1685
OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Taxonomic identifieri169963 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
ProteomesiUP000000817 Componenti: Chromosome

Organism-specific databases

GenoListiLMO1685.

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 – 432432Glutamate-1-semialdehyde 2,1-aminomutase 2PRO_0000120422Add
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

STRINGi169963.lmo1685.

Structurei

3D structure databases

ProteinModelPortaliQ8Y6J9.
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.
PhylomeDBiQ8Y6J9.

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.

Q8Y6J9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDHSMSKKLH DEALLHIVGG VNSPSRSNKG VGGGIPVTME RASGAYFYDV
60 70 80 90 100
DGNKYIDYLA AFGPIITGHA HPHITEAITK AAQNGVLYGT PTKHEITFAK
110 120 130 140 150
MLKEAIPSLE KVRFTNSGTE AVMTTIRVAR AYTGRDKIIK FAGCYHGHFD
160 170 180 190 200
LVLVEAGSGP STLGIPDSAG VTKSTAEEVI TVPFNDLDSF KEALAIWGDQ
210 220 230 240 250
VAAVLVEPIV GNFGMVAPED GFLEAVNELA HVNGSLVIYD EVITAFRFMY
260 270 280 290 300
GGAQNYLGVI PDLTAMGKII GGGLPIGAYG GRIDIMEKVA PLGPAYQAGT
310 320 330 340 350
HAGNPASILS GIACLEVLQE EGLYERFEKY GSMLKDGIEK AAAKHNIAVT
360 370 380 390 400
VNQIVGALTV YFTEDPVTNY AEAGATNGEL FGRFFKGMLE EGINLAPSKY
410 420 430
EAWFITSAHS EADILETIQA VDTVFGKMVQ DN
Length:432
Mass (Da):46,101
Last modified:February 28, 2002 - v1
Checksum:i127E7DA9790E8A61
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591980 Genomic DNA. Translation: CAC99763.1.
PIRiAE1285.
RefSeqiNP_465210.1. NC_003210.1.

Genome annotation databases

GeneIDi985629.
KEGGilmo:lmo1685.
PATRICi20312551. VBILisMon69206_1728.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591980 Genomic DNA. Translation: CAC99763.1.
PIRiAE1285.
RefSeqiNP_465210.1. NC_003210.1.

3D structure databases

ProteinModelPortaliQ8Y6J9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi169963.lmo1685.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi985629.
KEGGilmo:lmo1685.
PATRICi20312551. VBILisMon69206_1728.

Organism-specific databases

GenoListiLMO1685.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiFNDIDSY.
OrthoDBiEOG6QVRHN.
PhylomeDBiQ8Y6J9.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciLMON169963:LMO1685-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 nameiGSA2_LISMO
AccessioniPrimary (citable) accession number: Q8Y6J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 30, 2003
Last sequence update: February 28, 2002
Last modified: March 31, 2015
This is version 87 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.