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B0U0T6 (GSA_FRAP2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:Fphi_1812
OrganismFrancisella philomiragia subsp. philomiragia (strain ATCC 25017) [Complete proteome] [HAMAP]
Taxonomic identifier484022 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length433 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 – 433433Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000079923

Amino acid modifications

Modified residue2691N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0U0T6 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 0DDE792214244835

FASTA43347,506
        10         20         30         40         50         60 
MENKINSQSL FQEALQYIPG GVNSPVRAFK SVGQEFPRFI KSAKGAYLYD VDWNKYIDYI 

        70         80         90        100        110        120 
GSWGPMILGH GDDDVLEAIQ CQLKNGLSYG APCKQEIELA KKIVELMPNI EQVRFVNSGT 

       130        140        150        160        170        180 
EATMSAIRLA RAYTGRNKII KFEGCYHGHA DEFLVAAGSG ALSLGQPNSP GVPEDVVKDT 

       190        200        210        220        230        240 
LVASFNDIES IQALFEKYKN EIACIIVEPI AGNMNMIFPQ DDFLAKLRAV CDENNSLLIF 

       250        260        270        280        290        300 
DEVMTGFRVA LGGAQSIYDV KPDLTTLGKV IGGGMPVGAF GGRKEIMQEV SPAGPVYQAG 

       310        320        330        340        350        360 
TLSGNPIAMA AGIKTLEKVS QDDFFVKLEA KAKQLVDGLN EAARVYDFNF HAKYLGGMFG 

       370        380        390        400        410        420 
LFFCNEKVAV NTFTDLGKTN LKMFNKYFAY MLDNGVYLAP SAYEAGFISI AHSDEDIEKT 

       430 
ICLTKKFFQD NQS 

« Hide

References

[1]"Complete sequence of chromosome of Francisella philomiragia subsp. philomiragia ATCC 25017."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Richardson P.
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000937 Genomic DNA. Translation: ABZ88039.1.
RefSeqYP_001678540.1. NC_010336.1.

3D structure databases

ProteinModelPortalB0U0T6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING484022.Fphi_1812.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ88039; ABZ88039; Fphi_1812.
GeneID5908938.
KEGGfph:Fphi_1812.
PATRIC17940617. VBIFraPhi43880_1876.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycFPHI484022:GHVB-1866-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_FRAP2
AccessionPrimary (citable) accession number: B0U0T6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 44 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