ID   GSA_ECOSM               Reviewed;         426 AA.
AC   B1LGV7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000255|HAMAP-Rule:MF_00375};
DE            Short=GSA {ECO:0000255|HAMAP-Rule:MF_00375};
DE            EC=5.4.3.8 {ECO:0000255|HAMAP-Rule:MF_00375};
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000255|HAMAP-Rule:MF_00375};
DE            Short=GSA-AT {ECO:0000255|HAMAP-Rule:MF_00375};
GN   Name=hemL {ECO:0000255|HAMAP-Rule:MF_00375};
GN   OrderedLocusNames=EcSMS35_0166;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
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:0000255|HAMAP-Rule:MF_00375};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00375};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_00375}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00375}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00375}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00375}.
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DR   EMBL; CP000970; ACB16262.1; -; Genomic_DNA.
DR   RefSeq; WP_000045305.1; NC_010498.1.
DR   AlphaFoldDB; B1LGV7; -.
DR   SMR; B1LGV7; -.
DR   GeneID; 66671557; -.
DR   KEGG; ecm:EcSMS35_0166; -.
DR   HOGENOM; CLU_016922_1_5_6; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000007011; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR   InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00713; hemL; 1.
DR   PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR   PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Porphyrin biosynthesis; Pyridoxal phosphate.
FT   CHAIN           1..426
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_1000121886"
FT   MOD_RES         265
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   426 AA;  45340 MW;  4BD817E515468CF9 CRC64;
     MSKSENLYSA ARELIPGGVN SPVRAFTGVG GTPLFIEKAD GAYLYDVDGK AYIDYVGSWG
     PMVLGHNHPA IRNAVIEAAE RGLSFGAPTE MEVKMAQLVT ELVPTMDMVR MVNSGTEATM
     SAIRLARGFT GRDKIIKFEG CYHGHADCLL VKAGSGALTL GQPNSPGVPA DFAKHTLTCT
     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
//