ID   A4YDF0_METS5            Unreviewed;       417 AA.
AC   A4YDF0;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=4-aminobutyrate aminotransferase apoenzyme {ECO:0000313|EMBL:ABP94452.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABP94452.1};
GN   OrderedLocusNames=Msed_0275 {ECO:0000313|EMBL:ABP94452.1};
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549 {ECO:0000313|EMBL:ABP94452.1, ECO:0000313|Proteomes:UP000000242};
RN   [1] {ECO:0000313|EMBL:ABP94452.1, ECO:0000313|Proteomes:UP000000242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
RC   {ECO:0000313|Proteomes:UP000000242};
RX   PubMed=18083856; DOI=10.1128/AEM.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000682; ABP94452.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4YDF0; -.
DR   STRING; 399549.Msed_0275; -.
DR   KEGG; mse:Msed_0275; -.
DR   eggNOG; arCOG00915; Archaea.
DR   HOGENOM; CLU_016922_10_0_2; -.
DR   Proteomes; UP000000242; Chromosome.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ABP94452.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000242};
KW   Transferase {ECO:0000313|EMBL:ABP94452.1}.
SQ   SEQUENCE   417 AA;  45922 MW;  730C52FCAE8261AA CRC64;
     MSLASRIIEE DSRYLMQSFS RWYPLVIERA KGSLVYDVDG KEYIDMNAGI GVMALGHGNE
     KIIRAVQEQM NKFFHYSLTD FYYDLAVRVA RKLVSLVGFQ GKVFYANSGT ESVEASLKIA
     RGHTGRQYII GFTNSFHGRT FGSMSFTSSK SVQRSAFSPL LPSTLLVPYP DRHNPLCRED
     CANAVLEYIE DWVLKKIVDP NDVAGFLLEP IQGEGGIIVP PREFLQGLQR IARKNGILLI
     LDEVQTGIGR TGKMFAFEHF GVEPDLICLA KALGGGLPLG AVVGRSEVMD LPRGSHANTF
     GGNALALAAA EVVLEEVPGL LGRVNSLGKM IVDILGSTKS RYVEEIRGMG LMIGVDLRRD
     GEPYEEGLEK VLRRSFERGV LAIGAGESVV RLLPPLVIEE ELAQRGSSII REEIDRL
//