ID   GSA_MYCA9               Reviewed;         446 AA.
AC   B1MHH1;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=MAB_3978c;
OS   Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM
OS   13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacteroides; Mycobacteroides abscessus.
OX   NCBI_TaxID=561007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC   1543;
RX   PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA   Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA   Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA   Gaillard J.L.;
RT   "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT   Mycobacterium abscessus.";
RL   PLoS ONE 4:E5660-E5660(2009).
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; CU458896; CAM64052.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1MHH1; -.
DR   SMR; B1MHH1; -.
DR   EnsemblBacteria; CAM64052; CAM64052; MAB_3978c.
DR   KEGG; mab:MAB_3978c; -.
DR   OMA; AQTWRFP; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000007137; 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; 3.40.640.10; -; 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..446
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000382344"
FT   MOD_RES         281
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   446 AA;  46259 MW;  29D8BB3F6CEB6147 CRC64;
     MDDLASAETL DAVSDETPNS ARLFADASTV IPGGVNSPVR AFAAVGGVPR FVRSGAGCWL
     TDVDDNRYVD LVCSWGPLIL GHAHPAVVEA VQRAAKDGLS YGAPVEGEIE LAREIIDRVQ
     PVEKVRLVNS GTEATMSAVR LARGFTGRPK IVKFAGCYHG HADALLADAG SGLATFGLPS
     SPGVTGASAA DTIVLPYNDI GAVAQVFAEQ GDHIAAVITE AAAGNMGTVA PGPDFNAGLR
     RITENHGALL IMDEVMTGFR VSRSGWYGID QVAGDLVTFG KVMSGGMPAA AFGGRADIMD
     RLAPLGPVYQ AGTLSGNPVA VAAGLASLRA ADAKAYETLD RNADALIALL TASLDAEGVA
     HHIGRAGNMF SVFFGTEPVR DFQSAKATET WRYPAFFHGL LSRGVYPPAS AFETWFVSTA
     LDDEAFDRIA DALPAAARAA AAAEEN