ID   GSA_CLOK1               Reviewed;         422 AA.
AC   B9DZG0;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 73.
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=CKR_0584;
OS   Clostridium kluyveri (strain NBRC 12016).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=583346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12016;
RA   Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA   Yukawa H.;
RT   "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT   of Clostridia species.";
RL   Submitted (SEP-2005) 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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAH05635.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AP009049; BAH05635.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011989227.1; NC_011837.1.
DR   AlphaFoldDB; B9DZG0; -.
DR   SMR; B9DZG0; -.
DR   EnsemblBacteria; BAH05635; BAH05635; CKR_0584.
DR   KEGG; ckr:CKR_0584; -.
DR   HOGENOM; CLU_016922_1_5_9; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000007969; 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   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 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.
FT   CHAIN           1..422
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000382296"
FT   MOD_RES         264
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   422 AA;  46726 MW;  FAEAEDE075C78EA7 CRC64;
     MRNDKIFEES KLYMPGGVNS PVRAFKDVPL NPPVIKKGRG AYIYDEDGNE YIDFVCSWGP
     MILGHCDEDV VNAIKYTSEN AISFGATTKI ELELSKYICT TMDNIEMIRM VNSGTEATMS
     AVKLARGYTR RNKIIKFSGC YHGHFDDFLV EAGSGVMTEG IPGSAGVPKD SIKNTIIAEY
     NNLEDVKNIF NKYGSDTAAI IVEPVAGNMG VIPGRIDFLK GLRKLCDEYG SLLIFDEVMS
     GFRVAYKGAQ SLYGIKPDIT TMAKIMGGGL PCGAYGGRKD IMENLSPLGP VYQAGTMSGN
     PIVMAAGLAT LKKLNENPDY YVKLEKLGKK LEKGIKQISK DKNIPMVINR CGAMFSIFFT
     SDSEVKNYKD ARKCDTTIFA KFFQHMLERG IYIAPSQFEA IFLNVKHTEE HIDKFLQAVN
     TF