GSA1_BACMK
ID GSA1_BACMK Reviewed; 432 AA.
AC A9VSS7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase 1 {ECO:0000255|HAMAP-Rule:MF_00375};
DE Short=GSA 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00375};
DE Short=GSA-AT 1 {ECO:0000255|HAMAP-Rule:MF_00375};
GN Name=hemL1 {ECO:0000255|HAMAP-Rule:MF_00375};
GN OrderedLocusNames=BcerKBAB4_0447;
OS Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBAB4;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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}.
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DR EMBL; CP000903; ABY41713.1; -; Genomic_DNA.
DR RefSeq; WP_002125067.1; NC_010184.1.
DR AlphaFoldDB; A9VSS7; -.
DR SMR; A9VSS7; -.
DR STRING; 315730.BcerKBAB4_0447; -.
DR PRIDE; A9VSS7; -.
DR EnsemblBacteria; ABY41713; ABY41713; BcerKBAB4_0447.
DR KEGG; bwe:BcerKBAB4_0447; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_9; -.
DR OMA; NFGMVEP; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000002154; 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.
FT CHAIN 1..432
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase 1"
FT /id="PRO_0000382281"
FT MOD_RES 268
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ SEQUENCE 432 AA; 46280 MW; 0633563DF656DDDD CRC64;
MNFTKSEALH KEALEHIVGG VNSPSRSFKA VGGGSPVAME RGKGAYFWDV DGNKYIDYLA
AYGPIITGHA HPHITKAITT AAENGVLYGT PTALEVKFAK MLKEAMPALD KVRFVNSGTE
SVMTTIRVAR AYTGRTKIMK FAGCYHGHSD LVLVAAGSGP STLGTPDSAG VPQSIAQEVI
TVPFNNVETL KEALDKWGHE VAAILVEPIV GNFGIVEPKP GFLEKVNELV HEAGALVIYD
EVITAFRFMY GGAQDLLGVT PDLTALGKVI GGGLPIGAYG GKKEIMEQVA PLGPAYQAGT
MAGNPASMAS GIACLEVLQQ KGVYEKLDEL GAMLEKGILE QATKHNIDIT VNRLKGALTV
YFTTNTIEDY DAAKNTDGEM FGRFFKLMLQ EGINLAPSKY EAWFLTTEHT KEDIEYTIEA
VGRAFAALAD NK