Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23893 (GSA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Synonyms:gsa, popC
Ordered Locus Names:b0154, JW0150
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP-Rule MF_00375

Cofactor

Pyridoxal phosphate.

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.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00375.

Induction

Induced by low extracellular levels of magnesium via the PhoQ/PhoP two-component regulatory system. Ref.8

Sequence similarities

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

glcCP0ACL54EBI-909193,EBI-1115389

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000120408

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine Probable

Experimental info

Mutagenesis2651K → R: 2% of wild-type activity. Ref.7
Sequence conflict21S → R Ref.1
Sequence conflict21S → R Ref.2
Sequence conflict91S → Q Ref.1
Sequence conflict91S → Q Ref.2

Sequences

Sequence LengthMass (Da)Tools
P23893 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: BED817E100468CF2

FASTA42645,366
        10         20         30         40         50         60 
MSKSENLYSA ARELIPGGVN SPVRAFTGVG GTPLFIEKAD GAYLYDVDGK AYIDYVGSWG 

        70         80         90        100        110        120 
PMVLGHNHPA IRNAVIEAAE RGLSFGAPTE MEVKMAQLVT ELVPTMDMVR MVNSGTEATM 

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

       190        200        210        220        230        240 
YNDLASVRAA FEQYPQEIAC IIVEPVAGNM NCVPPLPEFL PGLRALCDEF GALLIIDEVM 

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

       310        320        330        340        350        360 
NPIAMAAGFA CLNEVAQPGV HETLDELTTR LAEGLLEAAE EAGIPLVVNH VGGMFGIFFT 

       370        380        390        400        410        420 
DAESVTCYQD VMACDVERFK RFFHMMLDEG VYLAPSAFEA GFMSVAHSME DINNTIDAAR 


RVFAKL 

« Hide

References

« Hide 'large scale' references
[1]"Structural genes of glutamate 1-semialdehyde aminotransferase for porphyrin synthesis in a cyanobacterium and Escherichia coli."
Grimm B., Bull A., Breu V.
Mol. Gen. Genet. 225:1-10(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
Fujita N., Mori H., Yura T., Ishihama A.
Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 2 AND 9.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"The Escherichia coli hemL gene encodes glutamate 1-semialdehyde aminotransferase."
Ilag L.L., Jahn D., Eggertsson G., Soell D.
J. Bacteriol. 173:3408-3413(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[7]"Activity and spectroscopic properties of the Escherichia coli glutamate 1-semialdehyde aminotransferase and the putative active site mutant K265R."
Ilag L.L., Jahn D.
Biochemistry 31:7143-7151(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-265.
[8]"Identification and molecular characterization of the Mg2+ stimulon of Escherichia coli."
Minagawa S., Ogasawara H., Kato A., Yamamoto K., Eguchi Y., Oshima T., Mori H., Ishihama A., Utsumi R.
J. Bacteriol. 185:3696-3702(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: K12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53696 Genomic DNA. Translation: CAA37734.1.
U00096 Genomic DNA. Translation: AAC73265.1.
AP009048 Genomic DNA. Translation: BAB96731.2.
U70214 Genomic DNA. Translation: AAB08584.1.
PIRB64739.
RefSeqNP_414696.1. NC_000913.3.
YP_488457.1. NC_007779.1.

3D structure databases

ProteinModelPortalP23893.
SMRP23893. Positions 1-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9886N.
IntActP23893. 2 interactions.
STRING511145.b0154.

Proteomic databases

PaxDbP23893.
PRIDEP23893.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73265; AAC73265; b0154.
BAB96731; BAB96731; BAB96731.
GeneID12931839.
946892.
KEGGecj:Y75_p0151.
eco:b0154.
PATRIC32115417. VBIEscCol129921_0160.

Organism-specific databases

EchoBASEEB0427.
EcoGeneEG10432. hemL.

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
PhylomeDBP23893.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycEcoCyc:GSAAMINOTRANS-MONOMER.
ECOL316407:JW0150-MONOMER.
MetaCyc:GSAAMINOTRANS-MONOMER.
UniPathwayUPA00251; UER00317.

Gene expression databases

GenevestigatorP23893.

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...

Other

PROP23893.

Entry information

Entry nameGSA_ECOLI
AccessionPrimary (citable) accession number: P23893
Secondary accession number(s): P78277
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 136 of the entry and version 2 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene