ID   GSA_METJA               Reviewed;         426 AA.
AC   Q58020;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   25-MAY-2022, entry version 127.
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; OrderedLocusNames=MJ0603;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB98593.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L77117; AAB98593.1; ALT_INIT; Genomic_DNA.
DR   PIR; C64375; C64375.
DR   RefSeq; WP_064496557.1; NC_000909.1.
DR   AlphaFoldDB; Q58020; -.
DR   SMR; Q58020; -.
DR   STRING; 243232.MJ_0603; -.
DR   EnsemblBacteria; AAB98593; AAB98593; MJ_0603.
DR   GeneID; 1451468; -.
DR   KEGG; mja:MJ_0603; -.
DR   eggNOG; arCOG00918; Archaea.
DR   HOGENOM; CLU_016922_1_5_2; -.
DR   InParanoid; Q58020; -.
DR   OMA; WGPLIFG; -.
DR   OrthoDB; 10264at2157; -.
DR   PhylomeDB; Q58020; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000000805; 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..426
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000120482"
FT   MOD_RES         266
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   426 AA;  47451 MW;  DDFFC01FCF52080C CRC64;
     MALKMDKSKE LFEEAKKYLV GGVNSPVRYF KPYPFFVEKA KDCYLFDVDG NCYIDYCLAY
     GPMVLGHAND AVIKAVKEQL ELGSAYGCPT EKEIILAKEV VKRVPCAEMV RFVNSGTEAT
     MSAIRLARGV TGRKKIIKFD GAYHGAHDYV LVKSGSGALT HGHPNSPGIP EETTKNTILI
     PFNDEDAVKK AINENKDEIA CIIVEPIMGN VGCILPKEGY LEFLREITEE NDILLIFDEV
     ITGFRLAKGG AQEYFGVVPD IATLGKILGG GFPIGAIVGR RELMEQFSPL GAIYQAGTFN
     GNPISITAGI ATLKQLDDRF YKETARTAKI LADTLRELAD KHNIKAKVYN IASMFQIYFN
     DKEVVNYEIA KQSDTEKFMK YFWRLLEKGV FVPPSQFECC FTSIKHDDEV VDKTIKAMED
     VFEGLE