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Q9JRW9 (GSA_CHLPN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 101. 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:CPn_0138, CP_0634, CpB0139
OrganismChlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]
Taxonomic identifier83558 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length440 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 – 440440Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000120399

Amino acid modifications

Modified residue2711N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Natural variant2571K → Q in strain: CWL029 and TW-183.

Sequences

Sequence LengthMass (Da)Tools
Q9JRW9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: BE2C04E0BA3E67CC

FASTA44047,956
        10         20         30         40         50         60 
MLNCSNQKHT VTFEEACQVF PGGVNSPVRA CRSVGVTPPI VSSAQGDIFL DTHGREFIDF 

        70         80         90        100        110        120 
CGGWGALIHG HSHPKIVKAI QKTALKGTSY GLTSEEEILF ATMLLSSLKL KEHKIRFVSS 

       130        140        150        160        170        180 
GTEATMTAVR LARGITNRSI IIKFIGGYHG HADTLLGGIS TTEETIDNLT SLIHTPSPHS 

       190        200        210        220        230        240 
LLISLPYNNS QILHHVMEAL GPQVAGIIFE PICANMGIVL PKAEFLDDII ELCKRFGSLS 

       250        260        270        280        290        300 
IMDEVVTGFR VAFQGAKDIF NLSPDITIYG KILGGGLPAA ALVGHRSILD HLMPEGTIFQ 

       310        320        330        340        350        360 
AGTMSGNFLA MATGHAAIQL CQSEGFYDHL SQLEALFYSP IEEEIRSQGF PVSLVHQGTM 

       370        380        390        400        410        420 
FSLFFTESAP TNFDEAKNSD VEKFQTFYSE VFDNGVYLSP SPLEANFISS AHTEENLTYA 

       430        440 
QNIIIDSLIK IFDSSAQRFF 

« Hide

References

[1]"Comparative genomes of Chlamydia pneumoniae and C. trachomatis."
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.
Nat. Genet. 21:385-389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CWL029.
[2]"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. expand/collapse author list , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AR39.
[3]"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J138.
[4]"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW-183.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001363 Genomic DNA. Translation: AAD18291.1.
AE002161 Genomic DNA. Translation: AAF38449.1.
BA000008 Genomic DNA. Translation: BAA98348.1.
AE009440 Genomic DNA. Translation: AAP98072.1.
PIRB86508.
F81555.
G72114.
RefSeqNP_224346.1. NC_000922.1.
NP_300197.1. NC_002491.1.
NP_445176.1. NC_002179.2.
NP_876415.1. NC_005043.1.

3D structure databases

ProteinModelPortalQ9JRW9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING115713.CPn0138.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD18291; AAD18291; CPn_0138.
AAF38449; AAF38449; CP_0634.
AAP98072; AAP98072; CpB0139.
BAA98348; BAA98348; BAA98348.
GeneID1466822.
894914.
918926.
963262.
KEGGcpa:CP0634.
cpj:CPj0138.
cpn:CPn0138.
cpt:CpB0139.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAPGFKPDI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00615.

Enzyme and pathway databases

BioCycCPNE115711:GI7B-655-MONOMER.
CPNE115713:GHEY-143-MONOMER.
CPNE138677:GH8N-141-MONOMER.
CPNE182082:GH4N-143-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 nameGSA_CHLPN
AccessionPrimary (citable) accession number: Q9JRW9
Secondary accession number(s): Q9Z945
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 101 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