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

A4XK09 (GSA_CALS8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:Csac_1654
OrganismCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]
Taxonomic identifier351627 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length427 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 – 427427Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000059979

Amino acid modifications

Modified residue2631N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4XK09 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: F5A073C54A26EF28

FASTA42747,012
        10         20         30         40         50         60 
MRFDKSKEIF DNTKRYIPGG VNSPVRAFKN LSITPPVISK GKGCRIFDID GNEYIDFVLS 

        70         80         90        100        110        120 
WGAMILGHCD PDVVNSIKEV VEDQIAFGAP TEIEYKMAKL VCETAQVDMV RFVNSGTEAT 

       130        140        150        160        170        180 
MTAIRLAKGY TGKKKIVKFA GCYHGHHDIF LKEAGSAVAE LRLKGIDEDI VQNTIVVEYN 

       190        200        210        220        230        240 
NLDSIEKAFK ENKDEISAVI IEPVAGNMGV VPAKKEFLQA LREICDLHGS LLIFDEVITG 

       250        260        270        280        290        300 
FRLSLKGARA LYNVEPDLVT FGKIIGGGLP CGAVGGKKEI MQCLAPQGNV FQAGTMSGNP 

       310        320        330        340        350        360 
IVMSAGYATI KKLKENPDIY TYLELLAQKL EGNLAKVFSS SNLTFCINRV GSMLTVFFGV 

       370        380        390        400        410        420 
EKVENFEMAK KSNLSMFKKF AEYMITNGIY IPSSQFEAMF LSSAHTESDI ERFAEVAEGF 


AKFVKKP 

« Hide

References

[1]"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903."
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., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43494 / DSM 8903.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000679 Genomic DNA. Translation: ABP67244.1.
RefSeqYP_001180435.1. NC_009437.1.

3D structure databases

ProteinModelPortalA4XK09.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351627.Csac_1654.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP67244; ABP67244; Csac_1654.
GeneID5088973.
KEGGcsc:Csac_1654.
PATRIC21253024. VBICalSac56748_1821.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCSAC351627:GJ17-1692-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_CALS8
AccessionPrimary (citable) accession number: A4XK09
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: February 19, 2014
This is version 49 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