ID A0A1G8LDV9_9BACI Unreviewed; 432 AA.
AC A0A1G8LDV9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05216352_108250 {ECO:0000313|EMBL:SDI53816.1};
OS Alteribacillus bidgolensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX NCBI_TaxID=930129 {ECO:0000313|EMBL:SDI53816.1, ECO:0000313|Proteomes:UP000199017};
RN [1] {ECO:0000313|EMBL:SDI53816.1, ECO:0000313|Proteomes:UP000199017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P4B,CCM 7963,CECT 7998,DSM 25260,IBRC-M 10614,KCTC 13821
RC {ECO:0000313|Proteomes:UP000199017};
RA de Groot N.N.;
RL Submitted (OCT-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|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}.
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DR EMBL; FNDU01000008; SDI53816.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8LDV9; -.
DR STRING; 930129.SAMN05216352_108250; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000199017; 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; 3.90.1150.10; 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:SF1; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 2; 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|ARBA:ARBA00022490, 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:UP000199017}.
FT MOD_RES 268
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00375"
SQ SEQUENCE 432 AA; 46526 MW; 0859E3886D2B0BAC CRC64;
MEKTHSEALY KEACEHIVGG VNSPSRSFKG VGGGTPIFME KGEGAYFYDV DGNKYIDYLG
AYGPIITGHA HPHITRAITN AAHNGTLYGT PTKLESQFAM MLKNSIPSLE KVRFVNSGTE
AVMTTIRVAR AYTGRTKVIK FAGCYHGHSD LVLVAAGSGP STLGSPDSAG VTKNIAEEVI
TVPFNDPENL KKALDKWGNE VAAVLVEPIV GNFGIVEPVP GFLETVNQLA HNAGSLVIYD
EVITAFRFMY GGAQNLLGVT PDMTAMGKII GGGLPIGAYG GRIDIMENVA PLGPAYQAGT
MSGNPASISA GIACLEVLQE EGVYEKLDYL GSRLEDGLNN IIKNHTVPAT VNRLKGALTL
YFTSQKVQNY DDADNSNDVL FSKFFKKMLN QGINLAPSKY EAWFITTAHE EKDIEETLKA
AEKAFDEIEK EQ
//
