GSA_NOCFA
ID GSA_NOCFA Reviewed; 445 AA.
AC Q5YP79;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=NFA_51600;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(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}.
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DR EMBL; AP006618; BAD60012.1; -; Genomic_DNA.
DR RefSeq; WP_011211694.1; NC_006361.1.
DR AlphaFoldDB; Q5YP79; -.
DR SMR; Q5YP79; -.
DR STRING; 247156.NFA_51600; -.
DR EnsemblBacteria; BAD60012; BAD60012; NFA_51600.
DR GeneID; 61135738; -.
DR KEGG; nfa:NFA_51600; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_11; -.
DR OMA; AQTWRFP; -.
DR BioCyc; NFAR247156:NFA_RS25590-MON; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000006820; 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..445
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000243590"
FT MOD_RES 276
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ SEQUENCE 445 AA; 45484 MW; 6B38484F7BE71817 CRC64;
MSASPRATHA SAAASARLFD RAAQVIPGGV NSPVRAFRSV GGTPRFIASA DGYTLTDADG
NEYVDLVCSW GPMILGHAHP AVVDAVRRAA TGGLSFGAPT EAEVELAEHI VARVAPVDRV
RLVNSGTEAT MSAVRLARGF TGRTKIIKFA GCYHGHVDAL LADAGSGVAT LGLPTSPGVT
GAQAADTIVL PYNDLDAVAA AFEANPGEIA CVITEAAAGN MGAVAPLPGF NAGLRELTEN
HGALLIMDEV MTGFRVSRSG WYGREGVAGD LYTFGKVMSG GLPAAAFGGR AEVMNQLAPL
GPVYQAGTLS GNPVAVAAGL ATLRAADDAV YAALDRNAER LGGLLTEALT AAGVEHQVQF
AGNMVSVFFS DRPVTDYATA KASQTWRFPA FFHALLDGGV YAPPSAFEAW FVSAALDEDA
FARIAAALPA AARAAAAATP EGSRA