ID   GSA_MYCLE               Reviewed;         446 AA.
AC   P46716;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 136.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase;
DE            Short=GSA;
DE            EC=5.4.3.8;
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase;
DE            Short=GSA-AT;
GN   Name=hemL; Synonyms=gsa; OrderedLocusNames=ML2414; ORFNames=B2168_C1_190;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U00018; AAA17225.1; -; Genomic_DNA.
DR   EMBL; AL583925; CAC31930.1; -; Genomic_DNA.
DR   PIR; S72889; S72889.
DR   RefSeq; NP_302563.1; NC_002677.1.
DR   RefSeq; WP_010908883.1; NC_002677.1.
DR   AlphaFoldDB; P46716; -.
DR   SMR; P46716; -.
DR   STRING; 272631.ML2414; -.
DR   EnsemblBacteria; CAC31930; CAC31930; CAC31930.
DR   KEGG; mle:ML2414; -.
DR   PATRIC; fig|272631.5.peg.4640; -.
DR   Leproma; ML2414; -.
DR   eggNOG; COG0001; Bacteria.
DR   HOGENOM; CLU_016922_1_5_11; -.
DR   OMA; AQTWRFP; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000000806; 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;
KW   Reference proteome.
FT   CHAIN           1..446
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000120424"
FT   MOD_RES         279
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   446 AA;  45790 MW;  1C684412C451FF6F CRC64;
     MGSTDQATAP AGPAVSISAK LFEDACAVIP GGVNSPVRAF SAVGGTPLFI TEARGCWLTD
     ADGRRYVDLV CSWGPMILGH AHPAVVDAVA TVAASGLSFG APTPAETQLA AEIIGRMAPV
     ERIRLVNSGT EATMSAVRLA RGFTGRTKII KFSGCYHGHV DALLADAGSG VATLSLPSSP
     GVTGAAAADT IVLPYNDIEA VRQTFARLGD QIAAVITEAS PGNMGVVPPA PGYNAALRAI
     TAEHGALLII DEVMTGFRVS RSGWYGLDPV AADLFIFGKV MSGGMPAAAF GGRAEVMERL
     APLGPVYQAG TLSGNPVAMA AGLATLRAAA DAVYATLDRN ADRLVAMLSE ALTDAGVPHQ
     IPRAGNMFSV FFSEAPVTDF ASACNSQVWR YPAFFHALLD AGVYPPCSTF EAWFVSAALD
     DAAFGRIVDA LPGAAAAAVA ARHRES