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B8FBA1 (GSA_DESAA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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:Dalk_2855
OrganismDesulfatibacillum alkenivorans (strain AK-01) [Complete proteome] [HAMAP]
Taxonomic identifier439235 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfatibacillum

Protein attributes

Sequence length425 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 – 425425Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382305

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B8FBA1 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 7183190967F6479A

FASTA42544,422
        10         20         30         40         50         60 
MEKSKELFAR ACKTIPGGVN SPVRACGSVG TDPCFIARGQ GSAIFDADGK QYIDYIGSWG 

        70         80         90        100        110        120 
PLILGHRHPA VIKAIEAALA NGCTFGAPTE LEIDLAEAVV NIMPSVEMVR MVNSGTEATM 

       130        140        150        160        170        180 
SAIRLARGAT GRDGIVKFDG CYHGHGDSLL VAAGSGVATL GIPGSPGVPD KVAESTASLE 

       190        200        210        220        230        240 
YNNIEAVKEY CKKKGDRTAA IIVEPVAGNM GVVAPKPEFI QGLREVCDQY GIVLILDEVM 

       250        260        270        280        290        300 
TGFRVALGGA QSLYGVTPDL TTMGKVIGGG LPVGAYGGKR SLMEKIAPSG PVYQAGTLSG 

       310        320        330        340        350        360 
NPMAMAAGIA TLKEISAPGF YEALEKSSQT LADGLKKAAA DAGVEAVISR VGSMQTLFFS 

       370        380        390        400        410        420 
AGPVENFEDA KKCDLDRFSK FYQGMRAEGV FLPPSQFEAW FVSSAHTEAD IEATLKAAEK 


VLRQL 

« Hide

References

[1]"Complete sequence of Desulfatibacillum alkenivorans AK-01."
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., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Wawrik B., Richardson P.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AK-01.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001322 Genomic DNA. Translation: ACL04545.1.
RefSeqYP_002432013.1. NC_011768.1.

3D structure databases

ProteinModelPortalB8FBA1.
SMRB8FBA1. Positions 2-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439235.Dalk_2855.

Proteomic databases

PRIDEB8FBA1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL04545; ACL04545; Dalk_2855.
GeneID7166792.
KEGGdal:Dalk_2855.
PATRIC21652402. VBIDesAlk8144_3051.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACGHANER.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycDALK439235:GHP2-2885-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_DESAA
AccessionPrimary (citable) accession number: B8FBA1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 39 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