ID   GSA_THEAB               Reviewed;         423 AA.
AC   B7IHH3;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 95.
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};
GN   OrderedLocusNames=THA_1081;
OS   Thermosipho africanus (strain TCF52B).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Thermosipho.
OX   NCBI_TaxID=484019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCF52B;
RX   PubMed=19124572; DOI=10.1128/jb.01448-08;
RA   Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA   Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT   "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT   the Firmicutes and Archaea.";
RL   J. Bacteriol. 191:1974-1978(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   -!- SUBUNIT: Homodimer. {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; CP001185; ACJ75537.1; -; Genomic_DNA.
DR   RefSeq; WP_012579987.1; NC_011653.1.
DR   AlphaFoldDB; B7IHH3; -.
DR   SMR; B7IHH3; -.
DR   STRING; 484019.THA_1081; -.
DR   KEGG; taf:THA_1081; -.
DR   eggNOG; COG0001; Bacteria.
DR   HOGENOM; CLU_016922_1_5_0; -.
DR   OrthoDB; 9801052at2; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000002453; 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.
FT   CHAIN           1..423
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000382387"
FT   MOD_RES         259
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   423 AA;  46921 MW;  2E1E249686DE3C17 CRC64;
     MFEIAKKYMP GGVNSPVRAF KSVEMEPIFV KSAKKSKLID INNKEYIDYI QSWGALILGH
     AHEEVVEEIK KQAELGTSYG LCHELEVEMA RLIVKHIPSV EMVRMVNSGT EAVMSAIRLA
     RAYTNRELIV KFEGCYHGHS DGLLVKAGSG ALTFGTPSSK GVTEKIVSNT LVARYNDIES
     VKELFDKYGE NIACVIVEPV AGNMGVVLPK QGFLEGLREI TKEYGSLLIF DEVITGFRVS
     INGAQGYYNV FPDITTLGKI IGGGLPVGAY GGRKEIMELI SPQGPVYQAG TLSGNPLTLA
     AGIKTIKIIE NDPDFYSKLD ELGKYFEEGI VSALGDFDVK INRIKSMLSF FFSKQEVDSY
     EKVINSDVEI YKKLFKCLFE NGILLPPSPF ESLFISSSHT KEDIEKTVYY FEKFSKKLKE
     GKV
//