ID   A0A1E7Q4T4_9GAMM        Unreviewed;       426 AA.
AC   A0A1E7Q4T4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   29-SEP-2021, entry version 19.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000256|HAMAP-Rule:MF_00375};
DE            Short=GSA {ECO:0000256|HAMAP-Rule:MF_00375};
DE            EC=5.4.3.8 {ECO:0000256|HAMAP-Rule:MF_00375};
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000256|HAMAP-Rule:MF_00375};
DE            Short=GSA-AT {ECO:0000256|HAMAP-Rule:MF_00375};
GN   Name=hemL {ECO:0000256|HAMAP-Rule:MF_00375};
GN   ORFNames=BI198_05335 {ECO:0000313|EMBL:OEY69058.1};
OS   Rheinheimera salexigens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=1628148 {ECO:0000313|EMBL:OEY69058.1, ECO:0000313|Proteomes:UP000242258};
RN   [1] {ECO:0000313|Proteomes:UP000242258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH87 {ECO:0000313|Proteomes:UP000242258};
RA   Wan X., Hou S.;
RL   Submitted (SEP-2016) 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:0000256|ARBA:ARBA00001579,
CC         ECO:0000256|HAMAP-Rule:MF_00375};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|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:0000256|ARBA:ARBA00004819}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00375}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily.
CC       {ECO:0000256|ARBA:ARBA00008981, ECO:0000256|HAMAP-Rule:MF_00375}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OEY69058.1}.
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DR   EMBL; MKEK01000001; OEY69058.1; -; Genomic_DNA.
DR   RefSeq; WP_070048624.1; NZ_MKEK01000001.1.
DR   EnsemblBacteria; OEY69058; OEY69058; BI198_05335.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000242258; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_00375};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00375};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW   Rule:MF_00375};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00375}; Reference proteome {ECO:0000313|Proteomes:UP000242258}.
FT   MOD_RES         265
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00375"
SQ   SEQUENCE   426 AA;  44990 MW;  AF7C41937BE02B33 CRC64;
     MSISEQLFAR AQRTIPGGVN SPVRAFSSVG GTPVFIDHAD GAYMFDVDGK RYIDYIGSWG
     PMLLGHNHPN IRQAVIDAAE KGLSFGAPCA AEVDMAEMVT KLVPSMEMVR MVSSGTEATM
     SAIRLARGYT NRNTIVKFEG CYHGHADSLL VKAGSGALTL GVPNSPGVPA DFAKYTLTCE
     FNNLAQLKQT FENHGDDIAC IIVEPVAGNM NCIPPAQGFL QGLRQLCDQY GAVLIFDEVM
     TGFRVALGGA QAFYDVKPDL TTLGKIIGGG MPVGAFGGKR EIMHHIAPLG PVYQAGTLSG
     NPIAMAAGLA SLTELSKPGV YEALTEKTRV LVSGIAAAAK KHGVPLATNQ VGAMFGLFFT
     TEANVSNFAQ ATQCDIAAFN RFFHLMLQQG VYLAPSAYEA GFISLAHSDA DIAHTIAAAE
     QSFAAL
//