GSA_ECOLI
ID GSA_ECOLI Reviewed; 426 AA.
AC P23893; P78277;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase;
DE Short=GSA;
DE EC=5.4.3.8 {ECO:0000269|PubMed:1643048, ECO:0000269|PubMed:2045363};
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase;
DE Short=GSA-AT;
GN Name=hemL; Synonyms=gsa, popC; OrderedLocusNames=b0154, JW0150;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1900346; DOI=10.1007/bf00282635;
RA Grimm B., Bull A., Breu V.;
RT "Structural genes of glutamate 1-semialdehyde aminotransferase for
RT porphyrin synthesis in a cyanobacterium and Escherichia coli.";
RL Mol. Gen. Genet. 225:1-10(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 2
RP AND 9.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=2045363; DOI=10.1128/jb.173.11.3408-3413.1991;
RA Ilag L.L., Jahn D., Eggertsson G., Soell D.;
RT "The Escherichia coli hemL gene encodes glutamate 1-semialdehyde
RT aminotransferase.";
RL J. Bacteriol. 173:3408-3413(1991).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF LYS-265.
RX PubMed=1643048; DOI=10.1021/bi00146a016;
RA Ilag L.L., Jahn D.;
RT "Activity and spectroscopic properties of the Escherichia coli glutamate 1-
RT semialdehyde aminotransferase and the putative active site mutant K265R.";
RL Biochemistry 31:7143-7151(1992).
RN [8]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=12813061; DOI=10.1128/jb.185.13.3696-3702.2003;
RA Minagawa S., Ogasawara H., Kato A., Yamamoto K., Eguchi Y., Oshima T.,
RA Mori H., Ishihama A., Utsumi R.;
RT "Identification and molecular characterization of the Mg2+ stimulon of
RT Escherichia coli.";
RL J. Bacteriol. 185:3696-3702(2003).
CC -!- FUNCTION: Aminomutase that catalyzes the transfer of the amine group on
CC carbon 2 of glutamate 1-semialdehyde to the adjacent carbon 1 to form
CC 5-aminolevulinate. {ECO:0000269|PubMed:1643048,
CC ECO:0000269|PubMed:2045363}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4-amino-5-oxopentanoate = 5-aminolevulinate;
CC Xref=Rhea:RHEA:14265, ChEBI:CHEBI:57501, ChEBI:CHEBI:356416;
CC EC=5.4.3.8; Evidence={ECO:0000269|PubMed:1643048,
CC ECO:0000269|PubMed:2045363};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14266;
CC Evidence={ECO:0000269|PubMed:1643048, ECO:0000269|PubMed:2045363};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:1643048, ECO:0000269|PubMed:2045363};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:2045363}.
CC -!- INTERACTION:
CC P23893; P0ACL5: glcC; NbExp=4; IntAct=EBI-909193, EBI-1115389;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by low extracellular levels of magnesium via the
CC PhoQ/PhoP two-component regulatory system.
CC {ECO:0000269|PubMed:12813061}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily. {ECO:0000305}.
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DR EMBL; X53696; CAA37734.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73265.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96731.2; -; Genomic_DNA.
DR EMBL; U70214; AAB08584.1; -; Genomic_DNA.
DR PIR; B64739; B64739.
DR RefSeq; NP_414696.1; NC_000913.3.
DR RefSeq; WP_000045315.1; NZ_LN832404.1.
DR AlphaFoldDB; P23893; -.
DR SMR; P23893; -.
DR BioGRID; 4260833; 31.
DR BioGRID; 851232; 2.
DR DIP; DIP-9886N; -.
DR IntAct; P23893; 2.
DR STRING; 511145.b0154; -.
DR jPOST; P23893; -.
DR PaxDb; P23893; -.
DR PRIDE; P23893; -.
DR EnsemblBacteria; AAC73265; AAC73265; b0154.
DR EnsemblBacteria; BAB96731; BAB96731; BAB96731.
DR GeneID; 946892; -.
DR KEGG; ecj:JW0150; -.
DR KEGG; eco:b0154; -.
DR PATRIC; fig|1411691.4.peg.2126; -.
DR EchoBASE; EB0427; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_6; -.
DR InParanoid; P23893; -.
DR OMA; WGPLIFG; -.
DR PhylomeDB; P23893; -.
DR BioCyc; EcoCyc:GSAAMINOTRANS-MON; -.
DR BioCyc; MetaCyc:GSAAMINOTRANS-MON; -.
DR UniPathway; UPA00251; UER00317.
DR PRO; PR:P23893; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00713; hemL; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isomerase; Porphyrin biosynthesis; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..426
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000120408"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305"
FT MUTAGEN 265
FT /note="K->R: 2% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:1643048"
FT CONFLICT 2
FT /note="S -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="S -> Q (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 45366 MW; BED817E100468CF2 CRC64;
MSKSENLYSA ARELIPGGVN SPVRAFTGVG GTPLFIEKAD GAYLYDVDGK AYIDYVGSWG
PMVLGHNHPA IRNAVIEAAE RGLSFGAPTE MEVKMAQLVT ELVPTMDMVR MVNSGTEATM
SAIRLARGFT GRDKIIKFEG CYHGHADCLL VKAGSGALTL GQPNSPGVPA DFAKYTLTCT
YNDLASVRAA FEQYPQEIAC IIVEPVAGNM NCVPPLPEFL PGLRALCDEF GALLIIDEVM
TGFRVALAGA QDYYGVVPDL TCLGKIIGGG MPVGAFGGRR DVMDALAPTG PVYQAGTLSG
NPIAMAAGFA CLNEVAQPGV HETLDELTTR LAEGLLEAAE EAGIPLVVNH VGGMFGIFFT
DAESVTCYQD VMACDVERFK RFFHMMLDEG VYLAPSAFEA GFMSVAHSME DINNTIDAAR
RVFAKL
