GSA1_BACP2
ID GSA1_BACP2 Reviewed; 431 AA.
AC A8FB92;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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}; OrderedLocusNames=BPUM_0825;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
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; CP000813; ABV61509.1; -; Genomic_DNA.
DR RefSeq; WP_012009345.1; NZ_VEIS01000018.1.
DR AlphaFoldDB; A8FB92; -.
DR SMR; A8FB92; -.
DR STRING; 315750.BPUM_0825; -.
DR EnsemblBacteria; ABV61509; ABV61509; BPUM_0825.
DR KEGG; bpu:BPUM_0825; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_9; -.
DR OMA; NFGMVEP; -.
DR OrthoDB; 493793at2; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000001355; 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..431
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase 1"
FT /id="PRO_0000382277"
FT MOD_RES 268
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ SEQUENCE 431 AA; 46615 MW; DD0209D464711692 CRC64;
MKFTESEKLH QEALEHIVGG VNSPSRSYKA VGGGSPVAME KGEGAYFWDV DGNRYIDYLA
AYGPIITGHA HPHITKAITK AAESGVLYGT PTKHEVTFAK MLKEAMPALD KVRFVNSGTE
AVMTTIRVAR AYTGRTKIIK FAGCYHGHSD LVLVAAGSGP STLGTPDSAG VPKSIANEVI
TVPFNDIDSY KEALDRWGDE VAAVLVEPIV GNFGIVEPKD GFLQQVNDLT HEKGALVIYD
EVITAFRFMY GGAQDLLQVK PDLTALGKII GGGLPIGAYG GKKEIMEQVA PLGPAYQAGT
MAGNPASILS GIACLEVLKQ DGVYERLDQL GAMLEEGILA HAKKHQVDIT VNRLKGALTV
YFTKETIVNY EQAENTDGEM FARFFKLMLS QGINLAPSKY EAWFLTIAHT EKDISETLQA
VDRAFEQLKQ S