ID   GSA_AQUAE               Reviewed;         424 AA.
AC   O66998;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 130.
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=aq_816;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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}.
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DR   EMBL; AE000657; AAC06964.1; -; Genomic_DNA.
DR   PIR; C70371; C70371.
DR   RefSeq; NP_213559.1; NC_000918.1.
DR   RefSeq; WP_010880497.1; NC_000918.1.
DR   AlphaFoldDB; O66998; -.
DR   SMR; O66998; -.
DR   STRING; 224324.aq_816; -.
DR   EnsemblBacteria; AAC06964; AAC06964; aq_816.
DR   KEGG; aae:aq_816; -.
DR   PATRIC; fig|224324.8.peg.644; -.
DR   eggNOG; COG0001; Bacteria.
DR   HOGENOM; CLU_016922_1_5_0; -.
DR   InParanoid; O66998; -.
DR   OMA; WGPLIFG; -.
DR   OrthoDB; 493793at2; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000000798; 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..424
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000120391"
FT   MOD_RES         264
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   424 AA;  46394 MW;  114DEF64E005E1E4 CRC64;
     MKNEKLYREA LQVMPGGVNS PVRAFKAVGG KPIFLVKGRG PRVWDAEGNE YIDFLASWGA
     IILGHAPKKV VKAVQEEAEK GLSFGLTNPH EVTLAKLVVE MVPSVEKVRF VNSGTEATMS
     AVRLARGVTG RKYIVKFEGC YHGHYDSLLV SAGSGVATFG IPGTPGIPEE IAKLTIVLPY
     NDVQALEEAF KEYGSEIAGV IVEPIAGNMG VVPPKKEFLI RLRELTKEYG SLLMFDEVIT
     GFRLSKGGAQ ELFGIEPDIT CLGKILGGGL PVGAYGGRRE IMERVAPEGE VYQAGTLAGN
     PLAMVSGSET LKDLRDKEPY KELEEKMEKL ARGVKDILTE KGIQHTINKV GSMMTVFFTD
     KKVVDFQTAK TSDTELFAKF FRALLNKGVL IPPSQFEAWF LTTAHEEEVI DEALERIRDA
     VKEL