GSA2_STAES
ID GSA2_STAES Reviewed; 429 AA.
AC Q8CRW7;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase 2 {ECO:0000255|HAMAP-Rule:MF_00375};
DE Short=GSA 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00375};
DE Short=GSA-AT 2 {ECO:0000255|HAMAP-Rule:MF_00375};
GN Name=hemL2 {ECO:0000255|HAMAP-Rule:MF_00375}; Synonyms=gsaB;
GN OrderedLocusNames=SE_1548;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05147.1; -; Genomic_DNA.
DR RefSeq; NP_765103.1; NC_004461.1.
DR RefSeq; WP_001830429.1; NZ_WBME01000089.1.
DR AlphaFoldDB; Q8CRW7; -.
DR SMR; Q8CRW7; -.
DR STRING; 176280.SE_1548; -.
DR EnsemblBacteria; AAO05147; AAO05147; SE_1548.
DR GeneID; 50018351; -.
DR KEGG; sep:SE_1548; -.
DR PATRIC; fig|176280.10.peg.1513; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_9; -.
DR OMA; NFGMVEP; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000001411; 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..429
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase 2"
FT /id="PRO_0000120455"
FT MOD_RES 268
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ SEQUENCE 429 AA; 47056 MW; 27C4F35B22E5B0DD CRC64;
MKFTESERLQ QLSNEYILGG VNSPSRSYKA VGGGAPVVMK EGHGAYLYDV DGNKYIDYLQ
AYGPIITGHA HPHITEAIQD QAAKGVLYGT PTELEINFSK KLREAVPSLE KIRFVNSGTE
AVMTTIRVAR AYTKRNKIIK FAGSYHGHSD LVLVAAGSGP SQLGSPDSAG VPQSVAQEVI
TVPFNDIESY REAIDYWKDD IAAVLVEPIV GNFGMVMPQP GFLEEVNKIS HDNGTLVIYD
EVITAFRFHY GAAQDLLGVK PDLTAFGKIV GGGLPIGGYG GRQDIMEHVA PLGPAYQAGT
MAGNPLSMRA GIALLEVLEQ EGVYDKLDQL GRRLEEGLQK LIDKHHITAT INRIYGSLTL
YFTNEKVTHY EQVENSDGDA FAQFFKLMLN QGINLAPSKF EAWFLTTEHT EEDIDRTLEA
ADYAFSKMK