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B4S0D0 (GSA_ALTMD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:MADE_1002445
OrganismAlteromonas macleodii (strain DSM 17117 / Deep ecotype) [Complete proteome] [HAMAP]
Taxonomic identifier314275 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

Protein attributes

Sequence length426 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 – 426426Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382249

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B4S0D0 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: D7DA4CD274FB9C55

FASTA42645,574
        10         20         30         40         50         60 
MQKSEALFTR AQKTIPGGVN SPVRAFKAVG GTPRFITKAD GAYMWDADGK QYIDYIQSWG 

        70         80         90        100        110        120 
PMILGHNNAP IREAVIEASC SGLSFGAPTE AEVIMAELVS EMVPSMEMVR MVNSGTEATM 

       130        140        150        160        170        180 
SAIRLARGYT SRNKIVKFEG CYHGHADSLL VKAGSGALTL GVPSSPGVPA NVAEHTLTVE 

       190        200        210        220        230        240 
FNNLDSVKEI FETHGDDIAC IIVEPVAGNM NCIPPVEGFL EGLRAICDQY GSVLIFDEVM 

       250        260        270        280        290        300 
TGFRVSRGGA QERFNVKPDL TCLGKVIGGG MPVGCFGGRR DIITHIAPTG PVYQAGTLSG 

       310        320        330        340        350        360 
NPVAMAAGLA ALTQIKQPGL YDSIFENTQA LVDGFQDLAD KHNISLTTNI AGSMFGIFFT 

       370        380        390        400        410        420 
DVEKVTNYKQ AINCNTEQFN KFYHGMLEQG VYLAPASYEA GFVSKAHDAE VIEKTLAAAD 


KVFSTL 

« Hide

References

[1]"Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
ISME J. 2:1194-1212(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17117 / Deep ecotype.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001103 Genomic DNA. Translation: AEA96638.1.
RefSeqYP_004425636.1. NC_011138.3.

3D structure databases

ProteinModelPortalB4S0D0.
SMRB4S0D0. Positions 2-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING314275.MADE_00484.

Proteomic databases

PRIDEB4S0D0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEA96638; AEA96638; MADE_1002445.
GeneID10555833.
KEGGamc:MADE_1002445.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
KOK01845.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycAMAC314275:GHA7-503-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_ALTMD
AccessionPrimary (citable) accession number: B4S0D0
Secondary accession number(s): F2G6G8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: September 1, 2009
Last modified: February 19, 2014
This is version 48 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