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Q9CNG9 (GSA_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 90. 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:PM0462
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella

Protein attributes

Sequence length427 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 – 427427Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000120429

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CNG9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: C15987BEE45206CA

FASTA42745,513
        10         20         30         40         50         60 
MTTSLSLFQR AQHRIPGGVN SPVRAFKGVG GTPIFIEKAQ GAYLYDTEGN QYIDYVGSWG 

        70         80         90        100        110        120 
PMILGHNHPT ILDAVISTAQ NGLSFGAPTA LEIELAELVC SLVPSIDMVR MVSSGTEATM 

       130        140        150        160        170        180 
SAIRLARGYT KRDKIIKFEG CYHGHADSLL VKAGSGALTL GQPSSPGVPA DFAKHTLTCT 

       190        200        210        220        230        240 
YNDLDSVKHA FEQYPNEIAC LIVEPVAGNM NCIPPQEGFL QGLRALCDQY GAVFIIDEVM 

       250        260        270        280        290        300 
TGFRVALGGA QTYYGVTPDL TCLGKVIGGG MPVGAFGGKK AIMQHIAPLG PVYQAGTLSG 

       310        320        330        340        350        360 
NPIAMAAGLA CLTELKKAGN AQRLAQQTEK LALGLKALAD KHHVPFVVNY VGGMFGIFFT 

       370        380        390        400        410        420 
EQKTVSSYQA VMACDTEKFN RFFHAMLAQG IYLAPSAFEA GFMSLAHSDQ DIERTLQAAD 


QVFSQLA 

« Hide

References

[1]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004439 Genomic DNA. Translation: AAK02546.1.
RefSeqNP_245399.1. NC_002663.1.

3D structure databases

ProteinModelPortalQ9CNG9.
SMRQ9CNG9. Positions 3-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272843.PM0462.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK02546; AAK02546; PM0462.
GeneID1243809.
KEGGpmu:PM0462.
PATRIC22870100. VBIPasMul88067_0474.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycPMUL272843:GC8W-474-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_PASMU
AccessionPrimary (citable) accession number: Q9CNG9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: February 19, 2014
This is version 90 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