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Q9PKI3 (GSA_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 95. 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:TC_0482
OrganismChlamydia muridarum (strain MoPn / Nigg) [Complete proteome] [HAMAP]
Taxonomic identifier243161 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length422 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 – 422422Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000120398

Amino acid modifications

Modified residue2581N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PKI3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C84505BB7EBBAF72

FASTA42246,158
        10         20         30         40         50         60 
MPHLFSKACQ YFPGGVNSPV RACRSVDITP PVVTRASGDF FTDSQGKTYI DFCGSWGSLI 

        70         80         90        100        110        120 
HGHSHPYICE AIQQGLQRGC SYGLTSEQEI SFAEEIFSYL EISNDHKIRF MSTGSEATMT 

       130        140        150        160        170        180 
AVRLARGVTE RPIIIKFSGC YHGHSDVFLQ EIHFQQTILD TVDLTQPLTL SLPFNNLSLF 

       190        200        210        220        230        240 
LDVMNQIGHR VAGVIFEPIC ANMGVVLPLP GFIEGIIQTC RKTGSLSIMD EVVTGFRVSK 

       250        260        270        280        290        300 
GGAAALHPLK PDILVFGKIL GGGLPASAVC APAAIMDYLA PVGKVFQAGT LSGNPLAMSA 

       310        320        330        340        350        360 
GKASIALCRE KNFYTQLSAI EDDFLSPIEQ MIQQSGIPVT LVRYGNLFSF FFSENRPNNL 

       370        380        390        400        410        420 
KEVQLCNTDI FRTFYQQAFL KGIYLSPSPF EASFLSTAHS MENLNYAQQV LIESLEQACS 


LV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39328.1.
PIRB81697.
RefSeqNP_296859.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PKI3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243161.TC0482.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF39328; AAF39328; TC_0482.
GeneID1245840.
KEGGcmu:TC_0482.
PATRIC20372396. VBIChlMur19118_0516.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00615.

Enzyme and pathway databases

BioCycCMUR243161:GHYU-501-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]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00713. hemL. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_CHLMU
AccessionPrimary (citable) accession number: Q9PKI3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 95 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