ID   GSA_SACS2               Reviewed;         418 AA.
AC   Q980U5; Q9UWG3;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   25-MAY-2022, entry version 119.
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=SSO0182;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-25, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP   REGULATION, AND SUBUNIT.
RC   STRAIN=DSM 5833 / MT-4;
RX   PubMed=8973563; DOI=10.1042/bj3200541;
RA   Palmieri G., Di Palo M., Scaloni A., Orru S., Marino G., Sannia G.;
RT   "Glutamate-1-semialdehyde aminotransferase from Sulfolobus solfataricus.";
RL   Biochem. J. 320:541-545(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; Evidence={ECO:0000255|HAMAP-Rule:MF_00375,
CC         ECO:0000269|PubMed:8973563};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00375,
CC         ECO:0000269|PubMed:8973563};
CC   -!- ACTIVITY REGULATION: Inhibited by gabaculine.
CC       {ECO:0000269|PubMed:8973563}.
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       ECO:0000269|PubMed:8973563}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK40528.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE006641; AAK40528.1; ALT_INIT; Genomic_DNA.
DR   PIR; A90159; A90159.
DR   AlphaFoldDB; Q980U5; -.
DR   SMR; Q980U5; -.
DR   STRING; 273057.SSO0182; -.
DR   EnsemblBacteria; AAK40528; AAK40528; SSO0182.
DR   KEGG; sso:SSO0182; -.
DR   PATRIC; fig|273057.12.peg.180; -.
DR   eggNOG; arCOG00918; Archaea.
DR   HOGENOM; CLU_016922_1_5_2; -.
DR   InParanoid; Q980U5; -.
DR   OMA; WGPLIFG; -.
DR   PhylomeDB; Q980U5; -.
DR   BRENDA; 5.4.3.8; 6163.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000001974; 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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Isomerase; Porphyrin biosynthesis;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..418
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000120490"
FT   MOD_RES         260
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
FT   CONFLICT        25
FT                   /note="A -> F (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   418 AA;  46477 MW;  C290C1884A38E710 CRC64;
     MNSEELWAQA KQLFAGGVNS PVRAAVKPFP FYVERGKGAY IYTVDGKKFI DYVLGYGPLI
     LGHSPESVKR RIVEQLERGW LFGTPSELEI ELARKIRSHI PSAQKIRFVN SGTEATMAAI
     RLARGYTKRS KILKFSGNYH GAHDYALVEA GSAATEYNVA TSDGVPMEIM KTVEICEFND
     LDCVDKKLRN EDIATVILEP VMGNAGVILP EKDFLFGLRE LTKTYNSLLI FDEVITGFRI
     SIGGAQSYYQ IYPDITTLGK IIGGGFPIGA VAGKAEIIDN FTPAGKVFNA GTFNANPISM
     IAGIATIEEL EKEYPYIIAN QAAKTLVEEL ERLLKTKHTI NHVGSMFQIF FGIDEVRNYS
     DAKRADKEYY IKFHERLLKE GVFIPPSQYE TIFTSAAHKD DVIADTIDKL MKVIGELN