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A9B550 (GSA_HERA2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:Haur_3551
OrganismHerpetosiphon aurantiacus (strain ATCC 23779 / DSM 785) [Complete proteome] [HAMAP]
Taxonomic identifier316274 [NCBI]
Taxonomic lineageBacteriaChloroflexiHerpetosiphonalesHerpetosiphonaceaeHerpetosiphon

Protein attributes

Sequence length429 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 – 429429Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000201023

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A9B550 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 35E675D4A76DC45F

FASTA42945,394
        10         20         30         40         50         60 
MINDASSAAF ERAQALLPGG VNSPVRAFRG VGGVPRFIDH GAGAYLYDID GNQYIDYVLS 

        70         80         90        100        110        120 
WGPLILGHAY PAVVEAICAQ AQRGTSFGAP TELESELAEL VIAAVPSVEM VRFVSSGTEA 

       130        140        150        160        170        180 
AMSAIRLARA YTQREKIIKF EGCYHGHADP FLVQAGSGVA TLGLPDSPGV LKSATSNTLT 

       190        200        210        220        230        240 
APFNDLEAVE ALFKANAGQV AALVIEPVAG NMGFVLPREG YLAGLRQLCD QYGALLIFDE 

       250        260        270        280        290        300 
VMTGFRVAYG GAQAYFNVMP DLTCLGKVVG GGLPAAAYGG RREIMQMVAP AGTMYQAGTL 

       310        320        330        340        350        360 
SGNPLAMVAG IVTLREIAKP EVFERLTGVT STLCQGFWKA AFKNGIPFQA HKAGSMWGFF 

       370        380        390        400        410        420 
FAGDEVYDFT SAKRADTAMF GKFFHAMLEQ GVYLAPSQFE AAFVSTAHTD ELVAQTINAA 


QAAFASIRS 

« Hide

References

[1]"Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Bryant D.A., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23779 / DSM 785.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000875 Genomic DNA. Translation: ABX06187.1.
RefSeqYP_001546315.1. NC_009972.1.

3D structure databases

ProteinModelPortalA9B550.
SMRA9B550. Positions 1-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316274.Haur_3551.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX06187; ABX06187; Haur_3551.
GeneID5735410.
KEGGhau:Haur_3551.
PATRIC22124263. VBIHerAur93466_3651.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycHAUR316274:GHYA-3588-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_HERA2
AccessionPrimary (citable) accession number: A9B550
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 55 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