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C1KVK0 (GSA1_LISMC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate-1-semialdehyde 2,1-aminomutase 1

Short name=GSA 1
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 1
Short name=GSA-AT 1
Gene names
Name:hemL1
Ordered Locus Names:Lm4b_01564
OrganismListeria monocytogenes serotype 4b (strain CLIP80459) [Complete proteome] [HAMAP]
Taxonomic identifier568819 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP-Rule MF_00375

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00375

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP-Rule MF_00375

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00375

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00375.

Sequence similarities

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

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

transaminase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 429429Glutamate-1-semialdehyde 2,1-aminomutase 1 HAMAP-Rule MF_00375
PRO_0000382334

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C1KVK0 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 9AFDE645956B60CB

FASTA42946,573
        10         20         30         40         50         60 
MQNYSKSEKA FKEAKKVLPG GVNSPVRAFN SVDASPVFMD HGKGAYITDV DGNEYIDYVL 

        70         80         90        100        110        120 
SWGPLILGHA DPAVVNAITK AALKGTSFGT PTEIETELAK LVIERVPSIE IVRMVSSGTE 

       130        140        150        160        170        180 
ATMSAIRLAR GYTKREKILK FEGSYHGHGD SLLIKAGSGV ATLGLPDSPG VTKGLAADTI 

       190        200        210        220        230        240 
TVPYNDIEGA ELAFQKYGEE IAAVIVEPVA GNMGVVPPID GFLEGLRELT TKFGSLLIFD 

       250        260        270        280        290        300 
EVMTGFRVDY YSAQGYYVVT PDLTCLGKVI GGGLPVGAYG GKKEIMEQIA PAGSIYQAGT 

       310        320        330        340        350        360 
LSGNPLAMNA GFETVRQLTP QHYDVFRTLI KRMEEGLTEI SARRQVPLSI NKAGSMFGFF 

       370        380        390        400        410        420 
FTDQKVINFD TAKTSNLEFF RNYYREMLGQ GIFLPPSQFE GVFISTMHTE KEIDKTLEAF 


DTTCKILRG 

« Hide

References

[1]"Comparative genomics and transcriptomics of lineages I, II, and III strains of Listeria monocytogenes."
Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B., Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A., Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P. expand/collapse author list , Rusniok C., Buchrieser C., Goebel W., Chakraborty T.
BMC Genomics 13:144-144(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CLIP80459.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM242711 Genomic DNA. Translation: CAS05325.1.
RefSeqYP_002758261.1. NC_012488.1.

3D structure databases

ProteinModelPortalC1KVK0.
SMRC1KVK0. Positions 36-425.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING634178.Lm4b_01564.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAS05325; CAS05325; Lm4b_01564.
GeneID7701630.
KEGGlmc:Lm4b_01564.
PATRIC20306295. VBILisMon88360_1574.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycLMON568819:GJF9-2309-MONOMER.
UniPathwayUPA00251; UER00317.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_00375. HemL_aminotrans_3.
InterProIPR004639. 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]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00713. hemL. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA1_LISMC
AccessionPrimary (citable) accession number: C1KVK0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 26, 2009
Last modified: May 14, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways