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A2BVE5 (GSA_PROM5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:P9515_05471
OrganismProchlorococcus marinus (strain MIT 9515) [Complete proteome] [HAMAP]
Taxonomic identifier167542 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

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

Porphyrin-containing compound metabolism; chlorophyll biosynthesis. 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.

Sequence caution

The sequence ABM71756.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processChlorophyll biosynthesis
Porphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processchlorophyll biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protoporphyrinogen 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_0000382359

Amino acid modifications

Modified residue2711N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A2BVE5 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: 5497134BEBF85809

FASTA43346,243
        10         20         30         40         50         60 
MTDIFNITHS EEVFSSALKL MPGGVSSPVR AFKSVGGQPI VFDRVKGPFA WDVDGNRYID 

        70         80         90        100        110        120 
YIGSWGPAIC GHAHPEVITA LQEAIEKGTS FGAPCVQENK LAEMVIDAVP SVEMVRFVNS 

       130        140        150        160        170        180 
GTEACMAVLR LMRAFTGRDK VIKFDGCYHG HADMFLVKAG SGVATLGLPD SPGVPRTTTA 

       190        200        210        220        230        240 
NTLTAPYNDL EAVKKLFSEN PDAISGVILE PIVGNAGFIT PEPGFLEGLR ELTTENGSLL 

       250        260        270        280        290        300 
VFDEVMTGFR ISYGGAQEKF GVTPDLTTLG KVIGGGLPVG AYGGRKEIMS MVAPSGPVYQ 

       310        320        330        340        350        360 
AGTLSGNPLA MTAGIKTLEL LKQEGTYEKM GLATSRLIEG IMQSAENNGI AINGGSVSAM 

       370        380        390        400        410        420 
FGFFLCEGPV RNFEEAKTNN SELFGKLHRE MIKRGVYLAP SPFEAGFTSL AHSEEEIDRT 

       430 
IEAFDQSFSV IKN 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9515.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000552 Genomic DNA. Translation: ABM71756.1. Different initiation.
RefSeqYP_001010863.1. NC_008817.1.

3D structure databases

ProteinModelPortalA2BVE5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167542.P9515_05471.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM71756; ABM71756; P9515_05471.
GeneID4719765.
KEGGpmc:P9515_05471.
PATRIC23014674. VBIProMar113831_0566.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycPMAR167542:GI3N-569-MONOMER.
UniPathwayUPA00251; UER00317.
UPA00668.

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_PROM5
AccessionPrimary (citable) accession number: A2BVE5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: September 1, 2009
Last modified: February 19, 2014
This is version 59 of the entry and version 2 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