ID   GSA_PYRAR               Reviewed;         423 AA.
AC   A4WN33;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=Pars_2254;
OS   Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=340102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
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   -!- 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; CP000660; ABP51800.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WN33; -.
DR   SMR; A4WN33; -.
DR   STRING; 340102.Pars_2254; -.
DR   EnsemblBacteria; ABP51800; ABP51800; Pars_2254.
DR   KEGG; pas:Pars_2254; -.
DR   HOGENOM; CLU_016922_1_5_2; -.
DR   OMA; WGPLIFG; -.
DR   PhylomeDB; A4WN33; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000001567; 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..423
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000382411"
FT   MOD_RES         258
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   423 AA;  46055 MW;  A5EAFB304C3B3F60 CRC64;
     MLFERARQVF PGGVNSPARA LKHLPSSLVA RAASGPYLYT DRGRLVDYCM AFGAIILGHA
     HPRVKRAVEE QLERGWIYAL LTEQEVEFAE AIRRHMPSVE KMRIVNTGTE ATMNAIRLAR
     GYTKRDVIIK FDGNFHGSHD YVLVKAGSGA ATWGIPTSAG VPQDVVKLTV VAPYNDVDAF
     LKAVKEVGDR LAAVIAEPVA GNYGLIIPDA EFLKALREET KRVGALLIFD EVITGFRLGL
     GGAQGRFGIR PDLTTLGKAV GGGFPIGIFG GRAEVMDLVA PSGPVYNAGT YNAHPVSVTA
     GLAVLKELET GEPFRTADEA AERLAKGIED IAGRLGFDVV VKKIASMFQF YFKKGDVKTP
     QDVRESNEKM YLKLHEIALR HGVYLTPSQF EVNFTSAAHT REVVEETLAA LEKAFQQLKT
     EIG