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C0QQ98 (GSA_PERMH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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:PERMA_1058
OrganismPersephonella marina (strain DSM 14350 / EX-H1) [Complete proteome] [HAMAP]
Taxonomic identifier123214 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesHydrogenothermaceaePersephonella

Protein attributes

Sequence length428 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 – 428428Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000201028

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C0QQ98 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: F6308798358CD7D1

FASTA42846,832
        10         20         30         40         50         60 
MKMERSLNLF EEAQRYLVGG VNSPVRAFKS VGMEPLFIQK GKGSRVWDVD GNEYIDYVLS 

        70         80         90        100        110        120 
WGPLILGHAN DQIVNAIKQV ANYGTSFGAP TELEIEMAKA VVDAVPSIEM VRFVNSGTEA 

       130        140        150        160        170        180 
TMSAIRLARG YTGKKKIVKF EGCYHGHVDS LLVSAGSGVA TLSIPGTPGI PEEFANLTIV 

       190        200        210        220        230        240 
LPYNNIDAVE ETFKKHGDDI ACVIIEPVAG NMGVVAPSKE YHQRLREITK EYGALLIWDE 

       250        260        270        280        290        300 
VMTGFRLAYG GAQELYGIEP DLTTLGKVIG GGLPVGAYGG KREIMEYVAP VGPVYQAGTL 

       310        320        330        340        350        360 
SGNPLAMAGG LRQLQILKEK NPYPDLDRKG KKLEEGLRYL SEKYGIPATV NRVGSMITAF 

       370        380        390        400        410        420 
FTDKEVVDFE TAKSSDLDRF AKFFRLMLEK GVYLAPSQFE AAFLSTAHSD EDIDETLNKA 


EDCFKQLL 

« Hide

References

[1]"Complete and draft genome sequences of six members of the Aquificales."
Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.
J. Bacteriol. 191:1992-1993(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14350 / EX-H1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001230 Genomic DNA. Translation: ACO04242.1.
RefSeqYP_002730844.1. NC_012440.1.

3D structure databases

ProteinModelPortalC0QQ98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING123214.PERMA_1058.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO04242; ACO04242; PERMA_1058.
GeneID7674806.
KEGGpmx:PERMA_1058.
PATRIC22915579. VBIPerMar119911_1096.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPMAR123214:GIZP-1057-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_PERMH
AccessionPrimary (citable) accession number: C0QQ98
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: February 19, 2014
This is version 40 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