ID   GSA_SULIL               Reviewed;         426 AA.
AC   C3MJ22;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=LS215_2116;
OS   Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=429572;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L.S.2.15 / Lassen #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(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   -!- 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; CP001399; ACP36109.1; -; Genomic_DNA.
DR   RefSeq; WP_012714102.1; NC_012589.1.
DR   AlphaFoldDB; C3MJ22; -.
DR   SMR; C3MJ22; -.
DR   EnsemblBacteria; ACP36109; ACP36109; LS215_2116.
DR   GeneID; 7809525; -.
DR   GeneID; 7939693; -.
DR   GeneID; 8762059; -.
DR   KEGG; sis:LS215_2116; -.
DR   HOGENOM; CLU_016922_1_5_2; -.
DR   OMA; WGPLIFG; -.
DR   OrthoDB; 10264at2157; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000001747; 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..426
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000382413"
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   426 AA;  47261 MW;  82BFEC7AB6396FA3 CRC64;
     MDKGRCTILN SEELWAQARQ LFAGGVNSPV RAAVKPFPFY VERGKGAYIY TVEGNKFIDY
     VLGYGPLILG HSPESVKRKI IEQLEKGWLF GTPSKLEIEL AKKISSHIPS AQKIRFVNSG
     TEATMAAIRL ARGYSKRSKI LKFSGNYHGA HDYTLVEAGS AATEYNVTTS DGIPMEIMKT
     VEICEFNDLD CVDKKLRNED IAAALLEPIM GNAGVILPEK GFLSGLRELT KSYNSLLIFD
     EVITGFRIDI GGAQSYYQIY PDITTLGKII GGGFPIGAVA GKAEIIDNFT PAGRVFNAGT
     FNANPISMIA GIATIEELEK EYPYNIANKA SKTLVEELER LLKIKHTINH IGSMFQVFFG
     IDKVRNYSDA KRANKEYYIK FHERLLKERV FIPPSQYETI FTSAAHEDDV VNDTIDKLAK
     VIGELS