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C1F911 (GSA_ACIC5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. 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:ACP_2074
OrganismAcidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670) [Complete proteome] [HAMAP]
Taxonomic identifier240015 [NCBI]
Taxonomic lineageBacteriaAcidobacteriaAcidobacterialesAcidobacteriaceaeAcidobacterium

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_0000382244

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C1F911 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 75F1C716960D63B1

FASTA42946,031
        10         20         30         40         50         60 
MIRSHMLRER AERLLPGGVD SPVRAFRAVG GEPPFLVKAE GACLWDADGN QYLDYFGSWG 

        70         80         90        100        110        120 
PMILGHAFPP VIEAIQKQAA FSTSFGASTP SEGDLAELVV RAYPSMEKLR FVSSGTEATM 

       130        140        150        160        170        180 
SALRLARAYT KRKYIVKFDG CYHGHSDGLL AKAGSGLATF GIPGSAGVPE EIAQLTLTLP 

       190        200        210        220        230        240 
FNNLDAVEAA FAAHRNEIAC IIVEPVAGNM GCVVPDEGYL QGLRELTRRE GALLIFDEVM 

       250        260        270        280        290        300 
TGFRVAFGGV QELRQVRPDL TTLGKIVGGG MPCGAFGGPA EIMDLLAPLG PVYQAGTLSG 

       310        320        330        340        350        360 
NPLAMAAGMA TVSHLESSKE WLYPQLEQMS AAVAQGVAEE AARAGIPLTT NRQGSMFTWF 

       370        380        390        400        410        420 
FTGQPVRDYA TAESCDTRRF AQFHRGMLDH GVWLPPSQFE AAFLGVAHTM HHVEQTVTAA 


REVFAAMQS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001472 Genomic DNA. Translation: ACO31495.1.
RefSeqYP_002755129.1. NC_012483.1.

3D structure databases

ProteinModelPortalC1F911.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING240015.ACP_2074.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO31495; ACO31495; ACP_2074.
GeneID7700842.
KEGGaca:ACP_2074.
PATRIC20667423. VBIAciCap40988_1994.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycACAP240015:GKF4-2029-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_ACIC5
AccessionPrimary (citable) accession number: C1F911
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 38 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