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Q1QSB0 (GSA_CHRSD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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

Short name=GSA
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name=GSA-AT
Gene names
Name:hemL
Ordered Locus Names:Csal_3304
OrganismChromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]
Taxonomic identifier290398 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHalomonadaceaeChromohalobacter

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 HAMAP-Rule MF_00375
PRO_0000300902

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1QSB0 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 32210269AE93656F

FASTA42945,522
        10         20         30         40         50         60 
MTTSAQLFEQ ACRHIPGGVN SPVRAFKGME RAPVFVERAQ GAYLYDVEGQ RYIDYVGSWG 

        70         80         90        100        110        120 
PLITGHADPD VLGAVRSRLD DGLSFGTPTA IETRMAELIC EIMPSIDMVR MVNSGTEATM 

       130        140        150        160        170        180 
SAIRLARGHT GRDKIVKFEG NYHGHSDSLL VKAGSGALTH GEPSSPGVPA SLAEHTVTLP 

       190        200        210        220        230        240 
YNDLDAVRAC FAELGDEIAG IIVEPVAGNM NCIPPQPDFL KGLREICDVH GSVLIFDEVM 

       250        260        270        280        290        300 
TGFRVALGGA QAHFGVTPDL TCLGKIVGGG MPVGAFGGTR EIMEQLSPLG PIYQAGTLAG 

       310        320        330        340        350        360 
NPLAMAAGIA LLEKIRQPGF HDALAERVAT LCDGLEARAR EAGVDLITQR AGGMFGVFFT 

       370        380        390        400        410        420 
AQQRVDNFAQ ATACNADTFR RFFLGMLEHG VYLAPSPFEA GFMSSAHTPD DIQATLDAAE 


QVLATLENA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000285 Genomic DNA. Translation: ABE60648.1.
RefSeqYP_575347.1. NC_007963.1.

3D structure databases

ProteinModelPortalQ1QSB0.
SMRQ1QSB0. Positions 3-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290398.Csal_3304.

Proteomic databases

PRIDEQ1QSB0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE60648; ABE60648; Csal_3304.
GeneID4028849.
KEGGcsa:Csal_3304.
PATRIC21450488. VBIChrSal113723_3321.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

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 nameGSA_CHRSD
AccessionPrimary (citable) accession number: Q1QSB0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 16, 2006
Last modified: May 14, 2014
This is version 58 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