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Q75G04 (GSA_LEPIC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. 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:LIC_20011
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) [Complete proteome] [HAMAP]
Taxonomic identifier267671 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length443 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 – 443443Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382331

Amino acid modifications

Modified residue2811N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q75G04 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 86211591A1EAA8D6

FASTA44348,527
        10         20         30         40         50         60 
MNQNKPTSKL ISDFWKGKTS EELFERAKKV SPGGVHSPVR SFRSVGGTPV FFASAKGATL 

        70         80         90        100        110        120 
TDISGKEYID YCLSFGPLIL GHRDPEIEEV VRETTEIAWS FGAAEPYSLE LAELISSRVP 

       130        140        150        160        170        180 
WAEKVRFVNS GTEAVMSALR VARAATGREK ILKFDGCYHG HLDSLLVKAG SGLAGESSSD 

       190        200        210        220        230        240 
SAGISATSIA NTLVLPLDDE ASVERVFETE GKNIAALIIE PLPANYGLLI QRKEFLLKIV 

       250        260        270        280        290        300 
ETARKYGTLV VFDEVISGFR VGFQGMSGLL GIWPDLVTYG KIIGGGFPVG CYAGKKDLLD 

       310        320        330        340        350        360 
LVAPSGPVYQ AGTLSANPFG MRAGLATLKK AQRDSIYSVL DDRTKIFTDT MTKLLNKKSN 

       370        380        390        400        410        420 
QEWEAVIHSS LFWFRKKTQQ PIRRIDLIPE GHKESFAKVF HTFLKNGIYL APSGYEVGFL 

       430        440 
SWAHDDEIIA KTLEIADKAL KTF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016824 Genomic DNA. Translation: AAS72040.1.
RefSeqYP_003403.1. NC_005824.1.

3D structure databases

ProteinModelPortalQ75G04.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267671.LIC20011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS72040; AAS72040; LIC_20011.
GeneID2769462.
KEGGlic:LIC20011.
PATRIC22380177. VBILepInt6257_4233.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycLINT267671:GHQI-3495-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.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_LEPIC
AccessionPrimary (citable) accession number: Q75G04
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 71 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