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P0CL07 (GSA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:STM0202
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length426 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.

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP-Rule MF_00375

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00375.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000120438

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0CL07 [UniParc].

Last modified March 8, 2011. Version 1.
Checksum: 40A283002A2D4B45

FASTA42645,325
        10         20         30         40         50         60 
MSKSENLYSA ARELIPGGVN SPVRAFTGVG GTPLFIEKAD GAYLYDVDGK AYIDYVGSWG 

        70         80         90        100        110        120 
PMVLGHNHPA IRNAVIEAAE RGLSFGAPTE MEVKMAELVT NLVPTMDMVR MVNSGTEATM 

       130        140        150        160        170        180 
SAIRLARGFT GRDKIIKFEG CYHGHADCLL VKAGSGALTL GQPNSPGVPA DFAKHTLTCT 

       190        200        210        220        230        240 
YNDLTSVRAA FEQYPQEIAS IIVEPVAGNM NCVPPLPEFL PGLRALCDEF GALLIIDEVM 

       250        260        270        280        290        300 
TGFRVALAGA QDYYGVVPDL TCLGKIIGGG MPVGAFGGRR DVMDALAPTG PVYQAGTLSG 

       310        320        330        340        350        360 
NPIAMAAGFA CLNEVAQPGI HETLDELTTR LAEGLCEAAQ EAGIPLVVNH VGGMFGIFFT 

       370        380        390        400        410        420 
DAESVTCYQD VMACDVERFK RFFHLMLEEG VYLAPSAFEA GFMSVAHSMD DINNTIDAAR 


RVFAKL

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence of the Salmonella typhimurium hemL gene and identification of the missing enzyme in hemL mutants as glutamate-1-semialdehyde aminotransferase."
Elliott T., Avissar Y.J., Rhie G.E., Beale S.I.
J. Bacteriol. 172:7071-7084(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Genomic subtraction identifies Salmonella typhimurium prophages and a novel fimbrial operon, stf, which are absent from S. typhi and E. coli."
Emmerth M., Goebel W., Miller S.I., Hueck C.J.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 378-426.
Strain: ATCC 14028s / SGSG 2262.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M60064 Genomic DNA. Translation: AAA63535.1.
AE006468 Genomic DNA. Translation: AAL19166.1.
AF093503 Genomic DNA. Translation: AAC64159.1.
PIRA37848.
RefSeqNP_459207.1. NC_003197.1.

3D structure databases

ProteinModelPortalP0CL07.
SMRP0CL07. Positions 2-422.
ModBaseSearch...

Proteomic databases

PRIDEP0CL07.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL19166; AAL19166; STM0202.
GeneID1251720.
KEGGstm:STM0202.
PATRIC32378689. VBISalEnt20916_0214.

Phylogenomic databases

HOGENOMHOG000020210.
KOK01845.
OMAFNGNPIS.

Enzyme and pathway databases

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.
PTHR11986:SF5. PTHR11986:SF5. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00713. hemL. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_SALTY
AccessionPrimary (citable) accession number: P0CL07
Secondary accession number(s): O87664, P21267
Entry history
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: March 8, 2011
Last modified: May 1, 2013
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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