ID   GSA_THEAC               Reviewed;         421 AA.
AC   Q9HKM6;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   27-MAR-2024, entry version 128.
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=Ta0571;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
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=CAC11711.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL445064; CAC11711.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048161655.1; NC_002578.1.
DR   AlphaFoldDB; Q9HKM6; -.
DR   SMR; Q9HKM6; -.
DR   STRING; 273075.gene:9571791; -.
DR   PaxDb; 273075-Ta0571; -.
DR   EnsemblBacteria; CAC11711; CAC11711; CAC11711.
DR   GeneID; 1456161; -.
DR   KEGG; tac:Ta0571; -.
DR   eggNOG; arCOG00918; Archaea.
DR   HOGENOM; CLU_016922_1_5_2; -.
DR   InParanoid; Q9HKM6; -.
DR   OrthoDB; 6524at2157; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000001024; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR   InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00713; hemL; 1.
DR   PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR   PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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..421
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000120492"
FT   MOD_RES         261
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   421 AA;  46430 MW;  02450AB01059FA89 CRC64;
     MGSKDLFQRG SSLFPMGVNS PVRYFKDYPF YVDNASGSRI YDVDGNEYID YCLAYGPSIL
     GHADPDVVRA VRDQAEKGLI YGAPSEAEIR LGDIIRRSSK NIEMMRFTNS GTEATMHAIR
     LARAYTGRSI IVKMEGGFHG AHDYSLIRSG SGTLTFGSPS SPGVPEEVAR TVVVGRYNDE
     ANIRNIFSQY GSRIAAVITE PIMGNAGVIT PEPGFLEFLR DITQKNGSLL IFDEVITGYR
     FAFSPYQDII GIRPDLTTMG KIIGGGMPIG LFGGSADIMK KVSPSGDVYQ SGTFSGNPVT
     MAAGFAALKK LQGMDYASLV RRTEKLMNGI DDILAKRKIR HVVNGYRSMF QFFFAESAKN
     YDEVMKADRD LYFRIFKRLM NHGVYVPPSQ FETNFVSFAH SDDDISKTIE AFDLSVGEAA
     K
//