ID   A0A1E7Q4T4_9GAMM        Unreviewed;       426 AA.
AC   A0A1E7Q4T4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   07-NOV-2018, entry version 10.
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;
OC   Chromatiaceae; Rheinheimera.
OX   NCBI_TaxID=1628148 {ECO:0000313|EMBL:OEY69058.1};
RN   [1] {ECO:0000313|EMBL:OEY69058.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KH87 {ECO:0000313|EMBL:OEY69058.1};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: (S)-4-amino-5-oxopentanoate = 5-
CC       aminolevulinate. {ECO:0000256|HAMAP-Rule:MF_00375,
CC       ECO:0000256|SAAS:SAAS01090807}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00375,
CC         ECO:0000256|SAAS:SAAS01090802};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step
CC       2/2. {ECO:0000256|SAAS:SAAS01090801}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00375}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375,
CC       ECO:0000256|SAAS:SAAS01090808}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00375, ECO:0000256|SAAS:SAAS01090804}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {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   UniPathway; UPA00251; UER00317.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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   ECO:0000256|SAAS:SAAS01090797};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00375,
KW   ECO:0000256|SAAS:SAAS01090803};
KW   Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00375,
KW   ECO:0000256|SAAS:SAAS01090799};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00375,
KW   ECO:0000256|RuleBase:RU003560, ECO:0000256|SAAS:SAAS01090798}.
FT   MOD_RES     265    265       N6-(pyridoxal phosphate)lysine.
FT                                {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
//