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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.

Cofactori

Pathway: protoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

GO - Molecular functioni

  • glutamate-1-semialdehyde 2,1-aminomutase activity Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • pyridoxal phosphate binding Source: InterPro
  • transaminase activity Source: InterPro

GO - Biological processi

  • protoporphyrinogen IX biosynthetic process Source: EcoCyc
  • tetrapyrrole biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:GSAAMINOTRANS-MONOMER.
ECOL316407:JW0150-MONOMER.
MetaCyc:GSAAMINOTRANS-MONOMER.
UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase (EC:5.4.3.8)
Short name:
GSA
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name:
GSA-AT
Gene namesi
Name:hemL
Synonyms:gsa, popC
Ordered Locus Names:b0154, JW0150
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10432. hemL.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi265 – 2651K → R: 2% of wild-type activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120408Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651N6-(pyridoxal phosphate)lysineCurated

Proteomic databases

PaxDbiP23893.
PRIDEiP23893.

Expressioni

Inductioni

Induced by low extracellular levels of magnesium via the PhoQ/PhoP two-component regulatory system.1 Publication

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
glcCP0ACL54EBI-909193,EBI-1115389

Protein-protein interaction databases

DIPiDIP-9886N.
IntActiP23893. 2 interactions.
STRINGi511145.b0154.

Structurei

3D structure databases

ProteinModelPortaliP23893.
SMRiP23893. Positions 1-426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
InParanoidiP23893.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.
PhylomeDBiP23893.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3.
InterProiIPR004639. 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]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23893-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKSENLYSA ARELIPGGVN SPVRAFTGVG GTPLFIEKAD GAYLYDVDGK
60 70 80 90 100
AYIDYVGSWG PMVLGHNHPA IRNAVIEAAE RGLSFGAPTE MEVKMAQLVT
110 120 130 140 150
ELVPTMDMVR MVNSGTEATM SAIRLARGFT GRDKIIKFEG CYHGHADCLL
160 170 180 190 200
VKAGSGALTL GQPNSPGVPA DFAKYTLTCT YNDLASVRAA FEQYPQEIAC
210 220 230 240 250
IIVEPVAGNM NCVPPLPEFL PGLRALCDEF GALLIIDEVM TGFRVALAGA
260 270 280 290 300
QDYYGVVPDL TCLGKIIGGG MPVGAFGGRR DVMDALAPTG PVYQAGTLSG
310 320 330 340 350
NPIAMAAGFA CLNEVAQPGV HETLDELTTR LAEGLLEAAE EAGIPLVVNH
360 370 380 390 400
VGGMFGIFFT DAESVTCYQD VMACDVERFK RFFHMMLDEG VYLAPSAFEA
410 420
GFMSVAHSME DINNTIDAAR RVFAKL
Length:426
Mass (Da):45,366
Last modified:November 1, 1997 - v2
Checksum:iBED817E100468CF2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → R (PubMed:1900346).Curated
Sequence conflicti2 – 21S → R (PubMed:8202364).Curated
Sequence conflicti9 – 91S → Q (PubMed:1900346).Curated
Sequence conflicti9 – 91S → Q (PubMed:8202364).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53696 Genomic DNA. Translation: CAA37734.1.
U00096 Genomic DNA. Translation: AAC73265.1.
AP009048 Genomic DNA. Translation: BAB96731.2.
U70214 Genomic DNA. Translation: AAB08584.1.
PIRiB64739.
RefSeqiNP_414696.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC73265; AAC73265; b0154.
BAB96731; BAB96731; BAB96731.
GeneIDi946892.
KEGGiecj:Y75_p0151.
eco:b0154.
PATRICi32115417. VBIEscCol129921_0160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53696 Genomic DNA. Translation: CAA37734.1.
U00096 Genomic DNA. Translation: AAC73265.1.
AP009048 Genomic DNA. Translation: BAB96731.2.
U70214 Genomic DNA. Translation: AAB08584.1.
PIRiB64739.
RefSeqiNP_414696.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP23893.
SMRiP23893. Positions 1-426.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9886N.
IntActiP23893. 2 interactions.
STRINGi511145.b0154.

Proteomic databases

PaxDbiP23893.
PRIDEiP23893.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73265; AAC73265; b0154.
BAB96731; BAB96731; BAB96731.
GeneIDi946892.
KEGGiecj:Y75_p0151.
eco:b0154.
PATRICi32115417. VBIEscCol129921_0160.

Organism-specific databases

EchoBASEiEB0427.
EcoGeneiEG10432. hemL.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
InParanoidiP23893.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.
PhylomeDBiP23893.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciEcoCyc:GSAAMINOTRANS-MONOMER.
ECOL316407:JW0150-MONOMER.
MetaCyc:GSAAMINOTRANS-MONOMER.

Miscellaneous databases

PROiP23893.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3.
InterProiIPR004639. 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]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiGSA_ECOLI
AccessioniPrimary (citable) accession number: P23893
Secondary accession number(s): P78277
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1997
Last modified: June 24, 2015
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.