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B9E740 (GSA1_MACCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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 1

Short name=GSA 1
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 1
Short name=GSA-AT 1
Gene names
Name:hemL1
Ordered Locus Names:MCCL_1301
OrganismMacrococcus caseolyticus (strain JCSC5402) [Complete proteome] [HAMAP]
Taxonomic identifier458233 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesMacrococcus

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 1 HAMAP-Rule MF_00375
PRO_0000382340

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B9E740 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 6393B1BB9E748849

FASTA42745,893
        10         20         30         40         50         60 
MDYSKSKQAF KEAVNLMPGG VNSPVRAFKS VDMDPIFMER GKGSKIYDID GNEYIDYVLS 

        70         80         90        100        110        120 
WGPLILGHAN DTVTGALNKA VLNGTSFGAP TELENKMAEL VIERVPSIEM VRMVSSGTEA 

       130        140        150        160        170        180 
TLAALRLARG FTGKNKILKF IGCYHGHSDS LLIKAGSGVA TLGLPDSPGV PKGTAENTIT 

       190        200        210        220        230        240 
VHYNDLDAVK LAFEQFGDDI AGVIVEPVAG NMGVVPPVEG FLEGLREITT EHGALLIFDE 

       250        260        270        280        290        300 
VMTGFRVGYN CAQGYFGVIP DLTCLGKVIG GGLPVGAFGG RKDIMEHIAP SGPVYQAGTL 

       310        320        330        340        350        360 
SGNPLAMTGG YYTLSQLTPE SYEYFNHLGD MLEAGLTDVF AKHNVPITIN RAGSMIGFFL 

       370        380        390        400        410        420 
NEEKVTNFEI ASKSDLKLFA AMYKEMANNG VFLPPSQFEG MFLSTEHTEE DIQKTINAFD 


NSLTVIL 

« Hide

References

[1]"Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402, reflecting the ancestral genome of the human-pathogenic staphylococci."
Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.
J. Bacteriol. 191:1180-1190(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC5402.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009484 Genomic DNA. Translation: BAH18008.1.
RefSeqYP_002560704.1. NC_011999.1.

3D structure databases

ProteinModelPortalB9E740.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING458233.MCCL_1301.

Proteomic databases

PRIDEB9E740.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH18008; BAH18008; MCCL_1301.
GeneID7389312.
KEGGmcl:MCCL_1301.
PATRIC22424989. VBIMacCas48391_1436.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARFMVSGN.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycMCAS458233:GI03-1313-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 nameGSA1_MACCJ
AccessionPrimary (citable) accession number: B9E740
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 43 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