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Q49Y99 (GSA2_STAS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. 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 2

Short name=GSA 2
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 2
Short name=GSA-AT 2
Gene names
Name:hemL2
Ordered Locus Names:SSP1097
OrganismStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) [Complete proteome] [HAMAP]
Taxonomic identifier342451 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

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 2 HAMAP-Rule MF_00375
PRO_0000243625

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q49Y99 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 499F5FAF6D63FE86

FASTA42746,146
        10         20         30         40         50         60 
MRYSNSEKAM AKAEELMPGG VNSPVRAFKS VDTPAIFMDH GEGSRIYDID GNEYIDYVLS 

        70         80         90        100        110        120 
WGPLILGHKN KQVIEKIHEA VDKGTSFGAS TLQENKLAEL VIERVPSIEK VRMVSSGTEA 

       130        140        150        160        170        180 
TLDTLRLARG YTGRNKIVKF VGCYHGHSDS LLIKAGSGVA TLGLPDSPGV PEGIAKNTIT 

       190        200        210        220        230        240 
VPYNDLDAIK VAFEEFGDDI AGVIVEPVAG NMGVVPPVEG FLQGLRDITT AYGSLLIFDE 

       250        260        270        280        290        300 
VMTGFRVGYN CAQGYFDVTP DLTCLGKVIG GGLPVGAFGG KKEIMDQIAP TGDIYQAGTL 

       310        320        330        340        350        360 
SGNPLAMTSG YETLSQLTPE TYDYFNKLGD LLEQGLKDVF AKHNVPITVN RAGSMIGYFL 

       370        380        390        400        410        420 
NAGPVTNFEQ ANNSDLEMFS QMYREMAKEG VFLPPSQFEG TFLSTSHTEE DINKTIQAFD 


TALSRIV 

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References

[1]"Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection."
Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.
Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15305 / DSM 20229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008934 Genomic DNA. Translation: BAE18242.1.
RefSeqYP_301187.1. NC_007350.1.

3D structure databases

ProteinModelPortalQ49Y99.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342451.SSP1097.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE18242; BAE18242; SSP1097.
GeneID3614939.
KEGGssp:SSP1097.
PATRIC19623778. VBIStaSap90642_1096.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSAP342451:GKFA-1156-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 nameGSA2_STAS1
AccessionPrimary (citable) accession number: Q49Y99
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 67 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