ID   GSA_CALMQ               Reviewed;         430 AA.
AC   A8M919;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=Cmaq_1413;
OS   Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS   IC-167).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Caldivirga.
OX   NCBI_TaxID=397948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Caldivirga maquilingensis IC-167.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; CP000852; ABW02238.1; -; Genomic_DNA.
DR   RefSeq; WP_012186457.1; NC_009954.1.
DR   AlphaFoldDB; A8M919; -.
DR   SMR; A8M919; -.
DR   STRING; 397948.Cmaq_1413; -.
DR   EnsemblBacteria; ABW02238; ABW02238; Cmaq_1413.
DR   GeneID; 5709309; -.
DR   KEGG; cma:Cmaq_1413; -.
DR   eggNOG; arCOG00918; Archaea.
DR   HOGENOM; CLU_016922_1_5_2; -.
DR   OMA; WGPLIFG; -.
DR   OrthoDB; 10264at2157; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000001137; 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..430
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000382392"
FT   MOD_RES         265
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   430 AA;  46993 MW;  6114E4FF30B6A80F CRC64;
     MATDAAELFK EALSLFPGGV NSPVRAMKHL PTPLIVKRAE GAFLYTIDGV KLIDYCMGFG
     PLILGHRHPT VLEAVRRSLE DGWLYGALTR NEVELAKEIN SSIRSVEMIR FVNTGTEAVM
     NAVRLARGFT GRRYIVKFEG NYHGAFDYVL VKAGSGAATW GVPTSAGILE DAVKYTLVVP
     YNDVEALERV FREHGSEIAL LLVEPIAGNY GLIIPDLEFI KATRELTERY GALLLFDEVI
     TGFRVGLNGA QGLFGIKPDL TTLGKIIGGG FPIGAFGGRR DVMSMITPQG PVYNAGTFNA
     HPVSVAAGLA TIRVIKSGGV YEVANEAAER ITEAILDSAS RSGFDIVVKR IASMFQFYFK
     KGDVKTPADV RASDEKLYLT FHREALSRGV YFTPSQYEVN FTSAAHSRDV VDETIRVIEE
     VFKALKTKAH