Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B9LTZ9 (GSA_HALLT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 37. 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:Hlac_2622
OrganismHalorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34) [Complete proteome] [HAMAP]
Taxonomic identifier416348 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalorubrum

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 – 445445Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000201041

Amino acid modifications

Modified residue2631N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B9LTZ9 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 2A33711268EF0CCF

FASTA44548,169
        10         20         30         40         50         60 
MNHERSRGLY DRALSVMPGG VNSSVRATMP HPFFIERGDG GHVIDADGNR YVDWVMGYGP 

        70         80         90        100        110        120 
LLYGHDLPDP VQAAIQSHVA AGPMYGAPTE IEVEHAEFVA RHVPSVESIR FVNSGTEATV 

       130        140        150        160        170        180 
SAVRLARGHT GRDKIVVMQG GYHGAQESTL VEGSPGDAHP STKGIPESFA EHTLPIPFND 

       190        200        210        220        230        240 
PQAAKKVFAE HGDDIAAVLV EPILANMGIV TPIDGYHETL RDLCDDHDSL LVFDEVITGF 

       250        260        270        280        290        300 
RVGGLGCAQS KFGVTPDVTT FGKIIGGGFP VGAIGGQAEI IEEFTPAGDV FQSGTFSGHP 

       310        320        330        340        350        360 
VTMAAGKASL EYAAENDVYE HVNRLGRKLR EGITEICTER APEYTVVGTD SMFKTIFTRD 

       370        380        390        400        410        420 
APDDPDACCA GGCRQNPDCD RYDTCPKNGA DVARAATDRW ERVFWQEMKE QGVFLTANQF 

       430        440 
ECQFTSYAHT EEDVEETLAA YREAI 

« Hide

References

[1]"Complete sequence of chromosome1 of Halorubrum lacusprofundi ATCC 49239."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N. expand/collapse author list , Anderson I., DasSarma S., Cavicchioli R., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001365 Genomic DNA. Translation: ACM58193.1.
RefSeqYP_002567263.1. NC_012029.1.

3D structure databases

ProteinModelPortalB9LTZ9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING416348.Hlac_2622.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM58193; ACM58193; Hlac_2622.
GeneID7399848.
KEGGhla:Hlac_2622.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.

Enzyme and pathway databases

BioCycHLAC416348:GIWW-2677-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. 2 hits.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_HALLT
AccessionPrimary (citable) accession number: B9LTZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 37 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