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A1KB59 (GSA_AZOSB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:azo3449
OrganismAzoarcus sp. (strain BH72) [Complete proteome] [HAMAP]
Taxonomic identifier62928 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAzoarcus

Protein attributes

Sequence length424 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 – 424424Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000300893

Amino acid modifications

Modified residue2661N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1KB59 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 7D0B7A43D7567D08

FASTA42444,404
        10         20         30         40         50         60 
MTSRNEALFS RAQRSIPGGV NSPVRAFRSV GGTPRFIERA EGARVWDADG KAYIDYVGSW 

        70         80         90        100        110        120 
GPAIAGHSHP AIVEAVREAA LRGLSFGAPT ESEVEMAELL CALLPSIEML RLVSSGTEAT 

       130        140        150        160        170        180 
MSAIRLARGF TGRDDIIKFE GCYHGHADSL LVKAGSGLLT FGNPSSGGVP ADFAHHTVVL 

       190        200        210        220        230        240 
DYNDLDQVET VFKARGDQIA AVIVEPVAGN MNLIKPRPGF LEGLRRLCTE YGAVLIFDEV 

       250        260        270        280        290        300 
MTGFRVGPQG VQGLYGITPD LTTLGKVIGG GMPVGAFGGR RDIMNCIAPL GPVYQAGTLS 

       310        320        330        340        350        360 
GSPVAVAAGL ASLRLTQAPG FYDALAARAR SLVDGLSGVA REAGVPFSAD SIGGMFGIYF 

       370        380        390        400        410        420 
SPSVPASFAE VMASDREAFN RFFHAMLDAG HYFAPSAFEA GFVSAAHGEA DIQATVAAAR 


ACLR 

« Hide

References

[1]"Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. strain BH72."
Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., Weidner S. expand/collapse author list , Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.
Nat. Biotechnol. 24:1385-1391(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BH72.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM406670 Genomic DNA. Translation: CAL96065.1.
RefSeqYP_934951.1. NC_008702.1.

3D structure databases

ProteinModelPortalA1KB59.
SMRA1KB59. Positions 3-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING62928.azo3449.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL96065; CAL96065; azo3449.
GeneID4607956.
KEGGazo:azo3449.
PATRIC21015350. VBIAzoSp26047_3493.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMALMAHIAP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

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_AZOSB
AccessionPrimary (citable) accession number: A1KB59
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 52 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