ID L7DZP3_MICAE Unreviewed; 433 AA.
AC L7DZP3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 ECO:0000313|EMBL:ELP52284.1};
GN ORFNames=O53_5179 {ECO:0000313|EMBL:ELP52284.1};
OS Microcystis aeruginosa TAIHU98.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Microcystaceae; Microcystis.
OX NCBI_TaxID=1134457 {ECO:0000313|EMBL:ELP52284.1, ECO:0000313|Proteomes:UP000010932};
RN [1] {ECO:0000313|EMBL:ELP52284.1, ECO:0000313|Proteomes:UP000010932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAIHU98 {ECO:0000313|EMBL:ELP52284.1,
RC ECO:0000313|Proteomes:UP000010932};
RX PubMed=23766403;
RA Yang C., Zhang W., Ren M., Song L., Li T., Zhao J.;
RT "Whole-Genome Sequence of Microcystis aeruginosa TAIHU98, a Nontoxic Bloom-
RT Forming Strain Isolated from Taihu Lake, China.";
RL Genome Announc. 1:e00333-13(2013).
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|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:ELP52284.1}.
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DR EMBL; ANKQ01000004; ELP52284.1; -; Genomic_DNA.
DR RefSeq; WP_002739946.1; NZ_ANKQ01000004.1.
DR AlphaFoldDB; L7DZP3; -.
DR PATRIC; fig|1134457.3.peg.4919; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000010932; 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:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00713; hemL; 1.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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}.
FT MOD_RES 273
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00375"
SQ SEQUENCE 433 AA; 45888 MW; CA977AE300E081C9 CRC64;
MVSTSSYQTT KSKEIFTAAQ KLMPGGVSSP VRAFKSVGGQ PIVFESVKGA YIRDVDGNEY
IDYVGTWGPA ICGHAHPEVI AALHQALDKG TSFGAPCVQE NILAEMVIDA VPSIEMVRFV
NSGTEACMSV LRLMRAFTGR DKIIKFEGCY HGHADMFLVK AGSGVATLGL PDSPGVPKTT
TNNTLTAPYN DLEAVKALFV ENPDSIAGVI LEPVVGNAGF IVPDAGFLEG LRELTKEYGA
LLMFDEVMTG FRIAYGGAQE KFGITPDLTT LGKVIGGGLP VGAYGGRADI MAMVAPAGPM
YQAGTLSGNP LAMTAGIKTL ELLQRPGTYE YLNKVTKSLT EGLLKVARDA GHSVSGGYIS
AMFGMFFTGS PVHNYEDAKK ADVAKFGRFH RGMLERGVYL APSQFEAGFT SLAHTEADIE
RTLAAAKEVL ASL
//
