ID   GSA_CROS5               Reviewed;         433 AA.
AC   B1X023;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 76.
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=cce_0172;
OS   Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS   ATCC 51142)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX   NCBI_TaxID=43989;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51142 / BH68;
RX   PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA   Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA   Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA   Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT   "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT   important in the marine nitrogen cycle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
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   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis. {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=ACB49524.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000806; ACB49524.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_024750185.1; NC_010546.1.
DR   AlphaFoldDB; B1X023; -.
DR   SMR; B1X023; -.
DR   STRING; 43989.cce_0172; -.
DR   EnsemblBacteria; ACB49524; ACB49524; cce_0172.
DR   KEGG; cyt:cce_0172; -.
DR   eggNOG; COG0001; Bacteria.
DR   HOGENOM; CLU_016922_1_5_3; -.
DR   OrthoDB; 493793at2; -.
DR   UniPathway; UPA00251; UER00317.
DR   UniPathway; UPA00668; -.
DR   Proteomes; UP000001203; Chromosome circular.
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:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniRule.
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   Chlorophyll biosynthesis; Cytoplasm; Isomerase; Porphyrin biosynthesis;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..433
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_0000382301"
FT   MOD_RES         273
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   433 AA;  45913 MW;  E1D73868664AB4C0 CRC64;
     MVSTTSLKTT KSEDIFAAAQ KLMPGGVSSP VRAFKSVGGQ PIVFDHVKGA YIWDVDGNQY
     IDYVGTWGPA ICGHAHPEVI AALHDALDRG TSFGAPCLLE NVLAEMVIDA VPSIEMVRFV
     NSGTEACMSV LRLMRAFTGR DKIIKFQGCY HGHADMFLVQ AGSGVATLGL PDSPGVPKTT
     TANTLTAPYN DLEAVKALFA ENPDEIAGVI LEPVVGNSGF VVPDGGFLQG LRELTNEYGA
     LLVFDEVMTG FRLSYGGAQE KFGVTPDLTT LGKVIGGGLP VGAYGGRKDI MSMVAPAGPM
     YQAGTLSGNP LAMTAGIKTL ELLQKPGTYN QLEQITQQLS EGLLKIAKEA GHQVCGGYIG
     AMFGLFFTEG PVRNYDDAKK SDLAKFGRFH RGMLEKGVYL APSQFEAGFT SLAHTSEDIE
     KTLAAAKDVL SNL