ID   GSA_MYCGI               Reviewed;         432 AA.
AC   A4T358;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 102.
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}; OrderedLocusNames=Mflv_0054;
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000656; ABP42550.1; -; Genomic_DNA.
DR   RefSeq; WP_011891058.1; NC_009338.1.
DR   AlphaFoldDB; A4T358; -.
DR   SMR; A4T358; -.
DR   STRING; 350054.Mflv_0054; -.
DR   EnsemblBacteria; ABP42550; ABP42550; Mflv_0054.
DR   KEGG; mgi:Mflv_0054; -.
DR   eggNOG; COG0001; Bacteria.
DR   HOGENOM; CLU_016922_1_5_11; -.
DR   OMA; WGPLIFG; -.
DR   OrthoDB; 493793at2; -.
DR   UniPathway; UPA00251; UER00317.
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; 3.40.640.10; -; 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   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Porphyrin biosynthesis; Pyridoxal phosphate.
FT   CHAIN           1..432
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000382345"
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   432 AA;  44410 MW;  F3B177B0F958CD1F CRC64;
     MSTTEESAKL FADASSVIPG GVNSPVRAFN SVGGTPRFIT SAKGCRLTDV DGNQYVDLVC
     SWGPMILGHA HPAVVEAVQR VAAHGLSFGA PTPSESELAR EIIDRVAPVE RVRLVNSGTE
     ATMSAIRLAR GFTGRAKIVK FSGCYHGHSD ALLADAGSGV ATLGLPSSPG VTGAAAADTL
     VLPYNNVAAV EEIFAQFGDE IACVITEASP GNMGTVPPLP GFNAALRRIT AAHGALLIVD
     EVMTGFRVSR SGWYGLDPVD ADLFTFGKVM SGGLPAAAFG GTAEVMGRLA PLGPVYQAGT
     LSGNPVAMAA GLATLRAADD AAYAKLDANA DRLVGLIGDA LTEAGVTHQI PRAGNMFSVF
     FGGDPVTDFA SAKATETWRF PAFFHALLDA GIYPPPSAYE AWFVSTALDD EAFDRIADAL
     PGAARAAAQA AA