ID A0A399JEJ8_9MICC Unreviewed; 438 AA.
AC A0A399JEJ8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:RII42599.1};
GN ORFNames=DWB68_06540 {ECO:0000313|EMBL:RII42599.1};
OS Galactobacter valiniphilus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Galactobacter.
OX NCBI_TaxID=2676122 {ECO:0000313|EMBL:RII42599.1, ECO:0000313|Proteomes:UP000265419};
RN [1] {ECO:0000313|EMBL:RII42599.1, ECO:0000313|Proteomes:UP000265419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JZ R-35 {ECO:0000313|EMBL:RII42599.1,
RC ECO:0000313|Proteomes:UP000265419};
RA Hahne J., Isele D., Lipski A.;
RT "Arthrobacter sp. nov., isolated from raw cow's milk with high bacterial
RT count.";
RL Submitted (JUL-2018) 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}.
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:RII42599.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QQXK01000010; RII42599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399JEJ8; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000265419; 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: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}; Reference proteome {ECO:0000313|Proteomes:UP000265419}.
FT MOD_RES 269
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00375"
SQ SEQUENCE 438 AA; 45236 MW; 34B18C65A41DA7C0 CRC64;
MTTNAQEFAS AQAIMPGGVN SPVRAFGSVG GVPPFLVDAH GAHVTDVEGK QYVDLVMSWG
PALLGHSHPA VIEAVHRAVD HGLSFGASTA DESKLARLIA NRMGGVERVR MVSTGTEATM
TAIRLARGYT GRDLVIKFAG NYHGHVDALL AAAGSGLATL ALPGSAGVPA AVTAETLVLP
YNNREALVAA FAEFGPRIAA VIAESAPCNM GVVAPEDGFN AYLREITAQH GSLLIIDEVL
TGFRASDAGY WGLTGRVEGW VPDLFTFGKV IGGGMPAAAI GGRQEVMEHL APLGPVYQAG
TLSGNPVATA AGIATLEHAS SEVYAHIDAR SLQLQDELTA AFNAAGVDHS IQVAGNLFSV
AFGTSDAGVH NYADAQAQEG WRYAPFFHSM LESGVYLPPS VFEAWFLSAA HDDAAMDRIV
SALPAAAAAA AAAEAPQD
//
