GSA_WIGBR
ID GSA_WIGBR Reviewed; 435 AA.
AC Q8D3C8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=WIGBR0730;
OS Wigglesworthia glossinidia brevipalpis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Wigglesworthia.
OX NCBI_TaxID=36870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12219091; DOI=10.1038/ng986;
RA Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA Aksoy S.;
RT "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT Wigglesworthia glossinidia.";
RL Nat. Genet. 32:402-407(2002).
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; BA000021; BAC24219.1; -; Genomic_DNA.
DR RefSeq; WP_011069877.1; NC_004344.2.
DR AlphaFoldDB; Q8D3C8; -.
DR SMR; Q8D3C8; -.
DR STRING; 36870.25166028; -.
DR EnsemblBacteria; BAC24219; BAC24219; BAC24219.
DR KEGG; wbr:hemL; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_6; -.
DR OMA; WGPLIFG; -.
DR OrthoDB; 493793at2; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000000562; 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..435
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000243642"
FT MOD_RES 270
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ SEQUENCE 435 AA; 48949 MW; FA0D7873C67BF683 CRC64;
MIKNSITNKL YVEAKKIIPG GVNSPARSFY FVKEIPVIAK RSKGPYIFDV DNNKYIDYIC
SWGASILGHN NYYITSKIIE YSKKGLNFGL LTEIEIKIAR LISKYIPSIE MIRMVNSGTE
ATMSAIRLAR SYTKKNKIIK FDGCYHGHAD FLLANSNLDP YDLFSSNPIS SGIPKNILKD
TLICPYNDYE SIEKIFDLYP NKIACIIVEP IAGNMGCVLP EKNFLYKLRM LCNKFNSLLI
MDEIITGFRI SLGGAQSYYN IYPDITCLGK IIGGGLPIGA FGGKKRIMNH VSPSGSVYQA
GTFSGNPISM ISGYACLKLL KSPDLYNKLN KKTEYLVNEL RSSACDNKIP VVINSLGSMF
SIFFTNLDKI KCYKDVSSCN YKKFILFFNE IKKLGILFSP SLFESNFITL MHKKKDLEKT
IDSANKVFKI LKNKV