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Q15YL3 (GSA_PSEA6) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:Patl_0495
OrganismPseudoalteromonas atlantica (strain T6c / ATCC BAA-1087) [Complete proteome] [HAMAP]
Taxonomic identifier342610 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

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_0000300935

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q15YL3 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 40F35C3E53335231

FASTA43146,062
        10         20         30         40         50         60 
MQKSEQLFAR AQKHIPGGVN SPVRAFRAVG GTPPFIEKAD GPYLYDADGK QYIDYVQSWG 

        70         80         90        100        110        120 
PMVLGHNNPI IRQAVIDAAQ NGLSFGAPTE AEVTIADLVS ELVPSMEMLR MVNSGTEATM 

       130        140        150        160        170        180 
SAIRLARGYT KRDKILKFEG CYHGHADALL VKAGSGALTF GVPSSPGIPA DFAKHTLTME 

       190        200        210        220        230        240 
YNNIDSVVQA FEQYPDDIAC IIVEPVAGNM NCIPPVHGFL QGLRDVCDKY GAVLIFDEVM 

       250        260        270        280        290        300 
TGFRVALGGA QAKYNIVPDL TCLGKVIGGG MPVGAFGGKR DIMQHIAPSG PVYQAGTLSG 

       310        320        330        340        350        360 
NPVAMAAGLA ALNQVKRPGL YEELSEATKT LAEGIKAIAN GLGIPMSVNY AGSMFGLFFT 

       370        380        390        400        410        420 
DVECVTNYQQ AINCNTEQFN HFYHGMLENG VYLAPASYEA GFVSAQHSPE IIQQTLQIAE 

       430 
KVLADVAKKF G 

« Hide

References

[1]"Complete sequence of Pseudoalteromonas atlantica T6c."
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T6c / ATCC BAA-1087.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000388 Genomic DNA. Translation: ABG39025.1.
RefSeqYP_660079.1. NC_008228.1.

3D structure databases

ProteinModelPortalQ15YL3.
SMRQ15YL3. Positions 2-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342610.Patl_0495.

Proteomic databases

PRIDEQ15YL3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG39025; ABG39025; Patl_0495.
GeneID4172722.
KEGGpat:Patl_0495.
PATRIC23045830. VBIPseAtl25434_0520.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPATL342610:GHGT-507-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_PSEA6
AccessionPrimary (citable) accession number: Q15YL3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 25, 2006
Last modified: February 19, 2014
This is version 58 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