GSA_THEAC
ID GSA_THEAC Reviewed; 421 AA.
AC Q9HKM6;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase;
DE Short=GSA;
DE EC=5.4.3.8;
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase;
DE Short=GSA-AT;
GN Name=hemL; OrderedLocusNames=Ta0571;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC11711.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AL445064; CAC11711.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048161655.1; NC_002578.1.
DR AlphaFoldDB; Q9HKM6; -.
DR SMR; Q9HKM6; -.
DR STRING; 273075.Ta0571; -.
DR EnsemblBacteria; CAC11711; CAC11711; CAC11711.
DR GeneID; 1456161; -.
DR KEGG; tac:Ta0571; -.
DR eggNOG; arCOG00918; Archaea.
DR HOGENOM; CLU_016922_1_5_2; -.
DR OMA; WGPLIFG; -.
DR OrthoDB; 10264at2157; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000001024; 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..421
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000120492"
FT MOD_RES 261
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 421 AA; 46430 MW; 02450AB01059FA89 CRC64;
MGSKDLFQRG SSLFPMGVNS PVRYFKDYPF YVDNASGSRI YDVDGNEYID YCLAYGPSIL
GHADPDVVRA VRDQAEKGLI YGAPSEAEIR LGDIIRRSSK NIEMMRFTNS GTEATMHAIR
LARAYTGRSI IVKMEGGFHG AHDYSLIRSG SGTLTFGSPS SPGVPEEVAR TVVVGRYNDE
ANIRNIFSQY GSRIAAVITE PIMGNAGVIT PEPGFLEFLR DITQKNGSLL IFDEVITGYR
FAFSPYQDII GIRPDLTTMG KIIGGGMPIG LFGGSADIMK KVSPSGDVYQ SGTFSGNPVT
MAAGFAALKK LQGMDYASLV RRTEKLMNGI DDILAKRKIR HVVNGYRSMF QFFFAESAKN
YDEVMKADRD LYFRIFKRLM NHGVYVPPSQ FETNFVSFAH SDDDISKTIE AFDLSVGEAA
K