ID   GSA_METHJ               Reviewed;         417 AA.
AC   Q2FTK5;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=Mhun_2560;
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD42259.1; -; Genomic_DNA.
DR   RefSeq; WP_011449516.1; NC_007796.1.
DR   AlphaFoldDB; Q2FTK5; -.
DR   SMR; Q2FTK5; -.
DR   STRING; 323259.Mhun_2560; -.
DR   EnsemblBacteria; ABD42259; ABD42259; Mhun_2560.
DR   GeneID; 3922817; -.
DR   KEGG; mhu:Mhun_2560; -.
DR   eggNOG; arCOG00918; Archaea.
DR   HOGENOM; CLU_016922_1_5_2; -.
DR   OMA; WGPLIFG; -.
DR   OrthoDB; 10264at2157; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000001941; 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..417
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000382409"
FT   MOD_RES         263
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   417 AA;  44370 MW;  87CE37FF3AF98598 CRC64;
     MSEKSREYYT IARDLMPGGV SSPVRAIQPY PFYTVRGSGS RIYTVDGTEL IDCCGAYGPL
     ILGHACKPVG DAISSALDDG WLYGTPTPAE IDLAQILIAD HPSIEMVRFV TTGSEATMAA
     IRLARGYTGK SDIIKTEGGF HGAHDGVLVQ AGSGCTTLGQ PDSAGVLSDI VRHTRQVPYN
     DTESLISLVD KSGDEIAAMI LEPVMGNIGP VLPKPGYLQE VRKITAEHDI LLIFDEVITG
     YRVGIGGAQK LFGVTPDITT LGKIIGGGLP LSAFGGKRKI MELIAPAGPV YQAGTFSGNP
     LSLAAGVAAL REIHARKGMY TLLDTATTVI GEACQGKGGS FVKLGSMFKF FFRSSVPENY
     AQAKESDTTK FRAFWEKMLE KGIFLPPSQF ETNFLSAAHS DSDVEYLSSA YASCLSA