GSA_HALWD
ID GSA_HALWD Reviewed; 446 AA.
AC Q18ES5;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=HQ_3447A;
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001;
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA Pfeiffer F., Oesterhelt D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM180088; CAJ53544.1; -; Genomic_DNA.
DR RefSeq; WP_011572639.1; NC_008212.1.
DR AlphaFoldDB; Q18ES5; -.
DR SMR; Q18ES5; -.
DR STRING; 362976.HQ_3447A; -.
DR EnsemblBacteria; CAJ53544; CAJ53544; HQ_3447A.
DR GeneID; 4194107; -.
DR KEGG; hwa:HQ_3447A; -.
DR eggNOG; arCOG00918; Archaea.
DR HOGENOM; CLU_016922_1_5_2; -.
DR OMA; WGPLIFG; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000001975; 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 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..446
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000382394"
FT MOD_RES 263
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ SEQUENCE 446 AA; 48496 MW; C72505354DAC3ADE CRC64;
MTDEESRALY DRALSVMPGG VNSSVRATQP YPFFIERGDG ATVIDADGTR YLDYVMGYGP
LLYGHDLPEP VNAAIQSYTS EGPMYGAPTP IEVEHAEFVA RHVPSVEMIR FVNSGTEATV
SAVRLARGYT GRDKIVVMKG GYHGAQESTL VEGDPMHVEP STPGIPSSFA KHTLPVPFND
LEAITTVFET HGEDIAAVLT EPILANNGIV RPVDGYLEHL RSLTTEHNSL LIFDEVITGF
RVGGLGCAQS KFGVTPDVTT FGKIIGGGFP VGAIGGRADI IEHFTPSGDV FQSGTFSGHP
VTMAAGYESL KYAAENDVYD HVNRLGERLR GGITDIATDQ SPSAIVVGLD SMFKTVFERE
GSTTDDGDVC SAGCEQRESC MRYDDCPKTG ADVSSAETER WERIFWQEMR DHNIFLTANQ
FESQFVSYAH TDEDIDRTLE AYKSAL