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A4SVE6 (GSA_POLSQ) 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:Pnuc_0239
OrganismPolynucleobacter necessarius subsp. asymbioticus (strain DSM 18221 / CIP 109841 / QLW-P1DMWA-1) [Complete proteome] [HAMAP]
Taxonomic identifier312153 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaePolynucleobacter

Protein attributes

Sequence length434 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 – 434434Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382358

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4SVE6 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: C27E7C3BEF3A3327

FASTA43446,486
        10         20         30         40         50         60 
MTKRDQNEVL FERAQKTIPG GVNSPVRAFR QVGGTPRFIS KAKGPYFWDA ENKRYIDLIM 

        70         80         90        100        110        120 
SWGPMIAGHA NPEVVEAVQK AAETSFSYGA PTEGEIELAE RICALVPSIE QVRMVSSGTE 

       130        140        150        160        170        180 
ATMSALRLAR GYTNRDLIIK FEGCYHGHAD SLLVKAGSGL LTFADSTQNA PSSGGVPQDL 

       190        200        210        220        230        240 
VKHTLVLPYN DVEAIEAVFK KQGNEIAAVI LEPIAGNMNL IKPSAEFLKA LRDLTSQYGS 

       250        260        270        280        290        300 
VLIYDEVMTG FRVALGGAQS LQGIVPDLTC LGKVMGGGMP MAAFGGKKEI MSKLAPLGNV 

       310        320        330        340        350        360 
YQAGTLSGNP VAVAAGLKTL EIVSRAGFYE CLSAQTEKLM LGLKQGADKS GIPFAVDSVG 

       370        380        390        400        410        420 
GMFGFYFADA VPSTYEAVTK TNIDAFKKFF HLMLDEGVYL APSAYEAGFT SIAHDDAVLQ 

       430 
VIIDAAEKSF PQLR 

« Hide

References

[1]"Complete genome sequence of Polynucleobacter necessarius subsp. asymbioticus type strain (QLW-P1DMWA-1(T))."
Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M., Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.
Stand. Genomic Sci. 6:74-83(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 18221 / CIP 109841 / QLW-P1DMWA-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000655 Genomic DNA. Translation: ABP33460.1.
RefSeqYP_001155024.1. NC_009379.1.

3D structure databases

ProteinModelPortalA4SVE6.
SMRA4SVE6. Positions 4-429.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING312153.Pnuc_0239.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP33460; ABP33460; Pnuc_0239.
GeneID5053619.
KEGGpnu:Pnuc_0239.
PATRIC22964827. VBIPolNec12025_0246.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAFADSTQN.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycPNEC312153:GH50-250-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_POLSQ
AccessionPrimary (citable) accession number: A4SVE6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 15, 2007
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