GSA_LEGPH
ID GSA_LEGPH Reviewed; 429 AA.
AC Q5ZVA6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=lpg1534;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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=AAU27616.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017354; AAU27616.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_015444486.1; NC_002942.5.
DR RefSeq; YP_095563.1; NC_002942.5.
DR AlphaFoldDB; Q5ZVA6; -.
DR SMR; Q5ZVA6; -.
DR STRING; 272624.lpg1534; -.
DR PaxDb; Q5ZVA6; -.
DR PRIDE; Q5ZVA6; -.
DR EnsemblBacteria; AAU27616; AAU27616; lpg1534.
DR GeneID; 66490664; -.
DR KEGG; lpn:lpg1534; -.
DR PATRIC; fig|272624.6.peg.1607; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_6; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000000609; 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..429
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000243582"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ SEQUENCE 429 AA; 46280 MW; B887BDE1A0892396 CRC64;
MSRSSDLFHK AQTIIPGGVN SPVRAFKGVG GEPVFFKSGK GAYLTDVDDK QYIDYVGSWG
PLILGHCHPK VIEAVDNVLH RGMSFGAPTE LEIQLAEKIA SLMPSIEKIR MVNSGTEATM
TAIRLARGFT NKNKFIKFNG CYHGHSDSLL VKAGSGLLTL GIPSTPGIPQ SITEHTLTAD
FNNLEQVAQL FEKYPNDIAT VILEPIPGNM GFILPKIEFL KGLRELCDQY NALLIFDEVM
TGFRVGLHGA QGLFGIKPDI TTLGKIIGGG MPVGALGGKR EIMSFLAPEG PVYQAGTLSG
NPLAMAAGLA TLKEIEKINF FEDLSNTTNK LTEALADAAE NANIPFFAAS LGGMFGFCFT
DKNSVENYLD VASSDEVLFK KFFHAMLAQG VYFAPSMYEA GFVSSMHGDL EIQKTYDAAE
LVLNQLKSA