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Q30RJ4 (GSA_SULDN) 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:Suden_1109
OrganismSulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251)) [Complete proteome] [HAMAP]
Taxonomic identifier326298 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeSulfurimonas

Protein attributes

Sequence length430 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 – 430430Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243639

Amino acid modifications

Modified residue2661N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q30RJ4 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 08CB736AA21D64DE

FASTA43045,790
        10         20         30         40         50         60 
MSIDNSLKAF KEAQNLIPGG VNSPVRAFKS VGGTPLFIAN GSGAYLTDID GNRYVDFVQS 

        70         80         90        100        110        120 
WGPLLFGHRD ESIESAVIEA VKHGLSFGAP TQAESDLAAL VISMFDSIEK IRFVSSGTEA 

       130        140        150        160        170        180 
VMSAIRLARG YTNCDDIVKF TGCYHGHSDS LLVQAGSGAA TFGNPSSPGV PADFTKHTLL 

       190        200        210        220        230        240 
AEYNNIESVK KCFSDSKDVA CVIIEPIAGN MGLVPADKEF LRELRELCDA NGALLIFDEV 

       250        260        270        280        290        300 
MSGFRASVHG AESITGVKPD IVTLGKVIGG GMPVGAFGAR AEIMAKLSPE GPVYQAGTLS 

       310        320        330        340        350        360 
GNPVAMAAGL AAITKLKQNG QIISVLNSRA TRLVEGMQEA AKTYGIAMQI DTRGSMFGFF 

       370        380        390        400        410        420 
FNEKPVKNFA DACNSDEKLF ALFHSKMLKE GFYFACSLYE TGFISTAITD EMIEDTIKAS 

       430 
AKVFKEITNV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000153 Genomic DNA. Translation: ABB44387.1.
RefSeqYP_393622.1. NC_007575.1.

3D structure databases

ProteinModelPortalQ30RJ4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326298.Suden_1109.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB44387; ABB44387; Suden_1109.
GeneID3763658.
KEGGtdn:Suden_1109.
PATRIC23770830. VBISulDen68967_1154.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAHGHANAF.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycSDEN326298:GH9P-1153-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_SULDN
AccessionPrimary (citable) accession number: Q30RJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 6, 2005
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