ID GSA1_LYSSC Reviewed; 429 AA.
AC B1HUT1;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 29-MAY-2013, entry version 47.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase 1;
DE Short=GSA 1;
DE EC=5.4.3.8;
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase 1;
DE Short=GSA-AT 1;
GN Name=hemL1; OrderedLocusNames=Bsph_0332;
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
OC Lysinibacillus.
OX NCBI_TaxID=444177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41;
RX PubMed=18296527; DOI=10.1128/JB.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J.,
RA Gao M., Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
CC -!- CATALYTIC ACTIVITY: (S)-4-amino-5-oxopentanoate = 5-
CC aminolevulinate.
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step
CC 2/2.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily.
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DR EMBL; CP000817; ACA37961.1; -; Genomic_DNA.
DR RefSeq; YP_001696091.1; NC_010382.1.
DR ProteinModelPortal; B1HUT1; -.
DR STRING; 444177.Bsph_0332; -.
DR EnsemblBacteria; ACA37961; ACA37961; Bsph_0332.
DR GeneID; 6020830; -.
DR KEGG; lsp:Bsph_0332; -.
DR PATRIC; 22413115; VBILysSph89750_0476.
DR eggNOG; COG0001; -.
DR HOGENOM; HOG000020210; -.
DR KO; K01845; -.
DR OMA; KVENYEQ; -.
DR ProtClustDB; PRK12389; -.
DR BioCyc; LSPH444177:GJEL-345-MONOMER; -.
DR UniPathway; UPA00251; UER00317.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:HAMAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:HAMAP.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 2.
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_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR PANTHER; PTHR11986; PTHR11986; 1.
DR PANTHER; PTHR11986:SF5; PTHR11986:SF5; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR TIGRFAMs; TIGR00713; hemL; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; FALSE_NEG.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Isomerase; Porphyrin biosynthesis;
KW Pyridoxal phosphate.
FT CHAIN 1 429 Glutamate-1-semialdehyde 2,1-aminomutase
FT 1.
FT /FTId=PRO_0000382338.
FT MOD_RES 268 268 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 429 AA; 45738 MW; 713570EA83CCA5BB CRC64;
MNHAKSEAVH AEALQHIVGG VNSPSRSYKA VGGGSPVAMV RGKGAYFWDV DGNRYIDYLA
AYGPIVTGHG HPHIAKAITH AAENGTLFGT PTEYEVTFAN MLKEAIPSMD KVRFNNSGTE
AVMTTIRVAR AYTGRTKIMK FAGCYHGHFD LVLVAAGSGP ATLGTPDSAG VTTSTAEEVI
TVPFNNPEAF TEAMNTWGDE IAAILIEPIV GNFGIVEPNP GFLELVHATA KEKGALTIYD
EVITAFRFHY GGAQNLLGLT PDLTALGKVI GGGLPIGAYG GRKEIMDTVA PLGPAYQAGT
MAGNPASMQA GIACLEVLQT PGIYDEMDRL GGILEEGILA AAKEHGVTIT LNRLKGALTI
YFTDVKVENY EQAENSNGEI FGRFFKLMLE QGVNLAPSKY EAWFLTTEHT EADILETIKA
VNYAFSQLS
//
