ID   GSA_FRATM               Reviewed;         431 AA.
AC   B2SGG7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=FTM_0885;
OS   Francisella tularensis subsp. mediasiatica (strain FSC147).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=441952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSC147;
RX   PubMed=19521508; DOI=10.1371/journal.ppat.1000472;
RA   Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T.,
RA   Keim P., Johansson A.;
RT   "Molecular evolutionary consequences of niche restriction in Francisella
RT   tularensis, a facultative intracellular pathogen.";
RL   PLoS Pathog. 5:E1000472-E1000472(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; CP000915; ACD30826.1; -; Genomic_DNA.
DR   RefSeq; WP_012429482.1; NC_010677.1.
DR   AlphaFoldDB; B2SGG7; -.
DR   SMR; B2SGG7; -.
DR   KEGG; ftm:FTM_0885; -.
DR   HOGENOM; CLU_016922_1_5_6; -.
DR   OMA; WGPLIFG; -.
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..431
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_1000121890"
FT   MOD_RES         269
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   431 AA;  47170 MW;  689E82630ADC4512 CRC64;
     MENKSNSQIL FAEAQQYIPG GVNSPVRAFK SVGQEFPRFI KFAKGAYLYD VDWNKYIDYI
     GSWGPMILGH CDDDVLEVIQ CQVKNGLSYG APCKQEVDLA KKIIELMPNI EQVRFVNSGT
     EATMSAIRLA RAYTCRNKII KFEGCYHGHA DEFLVAAGSG ALSLGQPNSP GVPEDVVKDT
     LVASFNDMES IQALFEKYKD EIACIIVEPI AGNMNMIFPQ DDFLAKLRAI CDQNSSLLIF
     DEVMTGFRVA LGGAQSIYNV KPDLTTLGKV IGGGMPVGAF GGRKEIMQKV SPAGPVYQAG
     TLSGNPIAMT AGIKTLEKIS QLGFFDELGA KAQKLVDGLN EAAKAYDFKF HAKCLGGMFG
     LFFCSDKIAV NTFVDLGKTN LKMFNQFFAY MLDNGVYLAP SAYEAGFISI AHSDEDIEKT
     ICLAKKFFQE N