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B7VJJ5 (GSA_VIBSL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:VS_2502
OrganismVibrio splendidus (strain LGP32) (Vibrio splendidus (strain Mel32)) [Complete proteome] [HAMAP]
Taxonomic identifier575788 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length431 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 – 431431Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000201039

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B7VJJ5 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 0DB3B5160DF44BF0

FASTA43146,065
        10         20         30         40         50         60 
MTKSAELYEK AQQTIPGGVN SPVRAFNGVG GSPIFVERAD GPLIFDADGK AYIDYVGSWG 

        70         80         90        100        110        120 
PMILGHNHVV IRDAVIAAAQ RGLSFGAPTE TEIKMAELVS EMVPSMEQLR MVSSGTEATM 

       130        140        150        160        170        180 
SAIRLARGFT GRDKILKFEG CYHGHADSLL VKAGSGALTL GQPSSPGVPA DFAKLTLTAT 

       190        200        210        220        230        240 
FNNLDSVREI FAANKGEIAC IIVEPVAGNM NCIPPVEGFH EGLREICDQE GALLIFDEVM 

       250        260        270        280        290        300 
TGFRVAEGCA QAYYNIKPDL TCLGKVIGGG MPVGAFGGRK DVMQYIAPTG PVYQAGTLSG 

       310        320        330        340        350        360 
NPVAMAAGYA CLNLLREEGN EKRLASKTKQ LANGFKQLAD KHGIPMLVHQ VGGMFGFFFT 

       370        380        390        400        410        420 
DQETVTCYED VTKCDVERFK RFFHLMLDHG VYLAPSAFEA SFTSLAHGSK ELDATLEAAD 

       430 
RSLAIIAAES K 

« Hide

References

[1]"Vibrio splendidus str. LGP32 complete genome."
Mazel D., Le Roux F.
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LGP32.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM954972 Genomic DNA. Translation: CAV19659.1.
RefSeqYP_002418084.1. NC_011753.2.

3D structure databases

ProteinModelPortalB7VJJ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING575788.VS_2502.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAV19659; CAV19659; VS_2502.
GeneID7162036.
KEGGvsp:VS_2502.
PATRIC20155578. VBIVibSpl48387_3760.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycVSPL575788:GH64-2461-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_VIBSL
AccessionPrimary (citable) accession number: B7VJJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: February 19, 2014
This is version 41 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