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A7I252 (GSA_CAMHC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:CHAB381_1034
OrganismCampylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A) [Complete proteome] [HAMAP]
Taxonomic identifier360107 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length450 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 – 450450Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000059981

Amino acid modifications

Modified residue2621N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7I252 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 59AA82B168C1CD24

FASTA45048,683
        10         20         30         40         50         60 
MSNHKEFSEA LKVIPGGVDS PVRAFKNVGS EPFMVQKGKG AYIYDIEGNK YLDFVQSWGP 

        70         80         90        100        110        120 
LIFGHADKDI QDAVIKTAKS GLSFGASSPL ETKLAKLILS KFDWLDKIRF VSSGTEATMS 

       130        140        150        160        170        180 
AIRLARGFSG KDKIIKFEGC YHGHSDSLLV KAGSGATTFG SSSSAGVPED TAKNTYLAIY 

       190        200        210        220        230        240 
NDIDSVKNIV EKEDIGTIII EPIAGNMGLV PADKEFLIKL RKICDEKKIV LILDEVMSGF 

       250        260        270        280        290        300 
RAGELGSYGI YGIKGDIVTF GKVIGGGMNV AAFAGKKEIM DMISPLGPVY QAGTLSGNPV 

       310        320        330        340        350        360 
SMAAGIASLT KIFASRNLYT KLENLANMFM IGLKNIAKNH GIAIQVAVRG SMFGYFFTDK 

       370        380        390        400        410        420 
AVKNYNDALS ADTKMFAKFH SGMIKEGIFL APSQFETGFI CDAMSEKEIN FALKKANKVF 

       430        440        450 
DEISKDSAKK ANKTKICSKK TVKKSVKNKK 

« Hide

References

[1]"Complete genome sequence of Campylobacter hominis ATCC BAA-381, a commensal isolated from the human gastrointestinal tract."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Nelson K.E.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000776 Genomic DNA. Translation: ABS51673.1.
RefSeqYP_001406593.1. NC_009714.1.

3D structure databases

ProteinModelPortalA7I252.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360107.CHAB381_1034.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS51673; ABS51673; CHAB381_1034.
GeneID5409668.
KEGGcha:CHAB381_1034.
PATRIC20040196. VBICamHom81367_0993.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAFADSTQN.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycCHOM360107:GHCX-1038-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_CAMHC
AccessionPrimary (citable) accession number: A7I252
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 47 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