GSA_LEPBJ
ID GSA_LEPBJ Reviewed; 441 AA.
AC Q04NV4;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=LBJ_4011;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB197;
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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 ---------------------------------------------------------------------------
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; CP000351; ABJ77416.1; -; Genomic_DNA.
DR RefSeq; WP_011671243.1; NC_008511.1.
DR AlphaFoldDB; Q04NV4; -.
DR SMR; Q04NV4; -.
DR EnsemblBacteria; ABJ77416; ABJ77416; LBJ_4011.
DR KEGG; lbj:LBJ_4011; -.
DR HOGENOM; CLU_016922_1_5_12; -.
DR OMA; WGPLIFG; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000000656; Chromosome 2.
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 PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; Porphyrin biosynthesis; Pyridoxal phosphate.
FT CHAIN 1..441
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000382328"
FT MOD_RES 279
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ SEQUENCE 441 AA; 48001 MW; 0C21B4B10699304B CRC64;
MSQRSSELIS DSWKGSSSEE LFERAKIVSP GGVHSPVRSF RSVGGTPVFF VSANGATLTD
VSGKEYVDFC LSFGPLILGH RDPEVEEVVR ETAGLAWSFG TAEPYSLELA EFITNRIPWA
EKVRFVNSGT EAVMSALRVT RAATGREKIF KFDGCYHGHL DALLVKAGSG LAGESSSDSA
GISSTAIANT LVLPLDDEMA VQKLFESEGK NIAALIIEPL PANYGLLVQR KEFLLKIVEI
AKKYGTLVVF DEVISGFRTG FQGMSGLLGI RPDLVTYGKI IGGGFPVGCY AGRRDLLDLV
APSGPVYQAG TLSANPFGMR AGLATLKKAE RDSIYSVLEV RTKTFADEMV KLLNGKTDQE
WEAVTHSSLF WFRKKTQQAV RRIDQIPEGH KEGFAEVFHV LLKNGIYLAP SGYEVGFLSW
AHNDSVIAKV LEIADKAFKE L