ID   GSA_CHLAA               Reviewed;         443 AA.
AC   A9WIS7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Caur_2598;
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX   PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA   Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA   Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA   Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT   "Complete genome sequence of the filamentous anoxygenic phototrophic
RT   bacterium Chloroflexus aurantiacus.";
RL   BMC Genomics 12:334-334(2011).
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}.
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DR   EMBL; CP000909; ABY35804.1; -; Genomic_DNA.
DR   RefSeq; WP_012258457.1; NC_010175.1.
DR   RefSeq; YP_001636193.1; NC_010175.1.
DR   AlphaFoldDB; A9WIS7; -.
DR   SMR; A9WIS7; -.
DR   STRING; 324602.Caur_2598; -.
DR   EnsemblBacteria; ABY35804; ABY35804; Caur_2598.
DR   KEGG; cau:Caur_2598; -.
DR   PATRIC; fig|324602.8.peg.2926; -.
DR   eggNOG; COG0001; Bacteria.
DR   HOGENOM; CLU_016922_1_5_0; -.
DR   InParanoid; A9WIS7; -.
DR   OMA; WGPLIFG; -.
DR   UniPathway; UPA00251; UER00317.
DR   UniPathway; UPA00668; -.
DR   Proteomes; UP000002008; 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: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..443
FT                   /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT                   /id="PRO_1000079915"
FT   MOD_RES         272
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   443 AA;  46746 MW;  963BA7CDC5AD6512 CRC64;
     MSVVTERYSR SQADYAAARE VIPGGVNSPV RAFRGVGGIP IFFERGQGAY VWDVDGNRYI
     DYVLSWGPLL LGHAHPAVVE AITLQAQRGT SFGAPTELET ELARLVIELV PSIEQIRFVN
     SGTEATMSAL RLARAATGRR LIVKFNGCYH GHADMLLVQA GSGVATLGLP DSPGVPPSVA
     AETITIEYND LDAAAALFAN RGAEIAAVIV EPIAANMGFV LPKPGFLSGL RELTQTHGAI
     FILDEVMTGF RVAAGGAQAL WGLDPDLTCL GKVIGGGLPV GAYAGKRQLM QLVAPAGPMY
     QAGTLSGNPL AMTAGLTTLR TAFGGDAGAF QQAVTRTARL ADGLRMLGER YRIPVQVGNV
     GTMFGCYFLR QEGSQITSYA EAKAYADSQR YARFFWAMAD QGIYLAPSQF EAGFLSTAHS
     DADIDETLAA AEVAFAGLVS SAE