GSA_DEIGD
ID GSA_DEIGD Reviewed; 446 AA.
AC Q1IWZ8;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000255|HAMAP-Rule:MF_00375};
DE Short=GSA {ECO:0000255|HAMAP-Rule:MF_00375};
DE EC=5.4.3.8 {ECO:0000255|HAMAP-Rule:MF_00375};
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000255|HAMAP-Rule:MF_00375};
DE Short=GSA-AT {ECO:0000255|HAMAP-Rule:MF_00375};
GN Name=hemL {ECO:0000255|HAMAP-Rule:MF_00375}; OrderedLocusNames=Dgeo_1942;
OS Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=319795;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11300 / AG-3a;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL Submitted (APR-2006) 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:0000255|HAMAP-Rule:MF_00375};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00375}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00375}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00375}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00375}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABF46236.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000359; ABF46236.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041221353.1; NC_008025.1.
DR AlphaFoldDB; Q1IWZ8; -.
DR SMR; Q1IWZ8; -.
DR STRING; 319795.Dgeo_1942; -.
DR EnsemblBacteria; ABF46236; ABF46236; Dgeo_1942.
DR KEGG; dge:Dgeo_1942; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_0; -.
DR OrthoDB; 493793at2; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000002431; Chromosome.
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; Isomerase; Porphyrin biosynthesis; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..446
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000382303"
FT MOD_RES 278
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ SEQUENCE 446 AA; 46789 MW; F0DD7B033FDB1C09 CRC64;
MTTQIRPFTT QSEALFARAQ AVTPGGVNSP VRAFRSVGGT PRFIREAHGA YLTDMDGHRL
LDYIGSWGPM ILGHDHPAVR EAVAAALDRG TSFGAPSEGE VRLAETVTRL TGVDRVRFVN
SGTEATMSAL RLARGFTGRT FIVKFRGNYH GHADGLLVEA GSGLMTNAAK TLGQAAPSSA
GVPEEYARLT LVCEYNDPAA LGALMQERGH DVAAVIFEPV VGNAGVLIPT PEFLAALHRV
RDAGALLIAD EVMTGFRLSL RGATGLLGLT PDLICWGKII GGGLPVGAYG GRAEVMDFVS
PQGPVYQAGT LSGNPLAMAA GLATLEVLES DPSIYARLET YTMQLAEGLR AAAQAAGVPL
SVNQIGSMLT AFHQDAPVGS IRTYADAARS DTGAFAVWFQ RMLAQGIYWA PSQFESIFVS
AAHTDSDLNA TLDAAHSAYA QLGGTA