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B8G2L6 (GSA_DESHD) 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:Dhaf_3348
OrganismDesulfitobacterium hafniense (strain DCB-2 / DSM 10664) [Complete proteome] [HAMAP]
Taxonomic identifier272564 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium

Protein attributes

Sequence length430 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 – 430430Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382306

Amino acid modifications

Modified residue2691N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B8G2L6 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: B1C040D8E1682326

FASTA43045,748
        10         20         30         40         50         60 
MGFQDQRSKE AFARANGVLP GGVNSPVRAF KSVGREPIFI AKGQGARLWD IDGNSYLDYV 

        70         80         90        100        110        120 
LSWGPLILGH AHPVVVGAIK AAAERGTSYG APTEIETECA EEVIKAFPSM EMVRMVSSGT 

       130        140        150        160        170        180 
EATMSALRLA RGVTGRNKII KFEGCYHGHG DSLLIKAGSG ALTFGVPTSP GVPSSVASQT 

       190        200        210        220        230        240 
IVAQYNDLEG LKEIFKECGE DIAAVILEPV TGNMGVVLPQ PGFLAGLRTL TQDYGSLLIF 

       250        260        270        280        290        300 
DEVMTGFRVS YGGAQGRYQI DPDLTCLGKV IGGGLPVAAY GGKRKYMEQV APSGPIYQAG 

       310        320        330        340        350        360 
TLSGNPLAMA AGLATLKLLQ QEGVYEGLEK KTARLAEGLQ SIAQELGFPI WVNSVGAMFS 

       370        380        390        400        410        420 
AFFTDQPVID FKSACSSDVE RFGSFFRGML ERGIYLAPSQ YEAVFLSAAH TDADIDYTLE 

       430 
QARDVLKSLG 

« Hide

References

[1]"Complete sequence of Desulfitobacterium hafniense DCB-2."
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., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ovchinnikova G., Madsen T., Christiansen N., Ahring B., Marsh T., Harzman C., Davis J.K., Kim S.-H., Tiedje J.M.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DCB-2 / DSM 10664.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001336 Genomic DNA. Translation: ACL21366.1.
RefSeqYP_002459802.1. NC_011830.1.

3D structure databases

ProteinModelPortalB8G2L6.
SMRB8G2L6. Positions 4-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272564.Dhaf_3348.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL21366; ACL21366; Dhaf_3348.
GeneID7260365.
KEGGdhd:Dhaf_3348.
PATRIC21664657. VBIDesHaf15223_3488.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycDHAF272564:GCV8-3421-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_DESHD
AccessionPrimary (citable) accession number: B8G2L6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: March 3, 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