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Database: UniProt
Entry: Q6L0X6_PICTO
LinkDB: Q6L0X6_PICTO
Original site: Q6L0X6_PICTO 
ID   Q6L0X6_PICTO            Unreviewed;       448 AA.
AC   Q6L0X6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AAT43376.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:AAT43376.1};
GN   OrderedLocusNames=PTO0791 {ECO:0000313|EMBL:AAT43376.1};
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828 / KAW 2/3).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=1122961 {ECO:0000313|EMBL:AAT43376.1, ECO:0000313|Proteomes:UP000000438};
RN   [1] {ECO:0000313|EMBL:AAT43376.1, ECO:0000313|Proteomes:UP000000438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
RC   {ECO:0000313|Proteomes:UP000000438};
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Futterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT43376.1; -; Genomic_DNA.
DR   RefSeq; WP_011177592.1; NC_005877.1.
DR   AlphaFoldDB; Q6L0X6; -.
DR   STRING; 263820.PTO0791; -.
DR   PaxDb; 263820-PTO0791; -.
DR   GeneID; 2844087; -.
DR   KEGG; pto:PTO0791; -.
DR   PATRIC; fig|263820.9.peg.826; -.
DR   eggNOG; arCOG00915; Archaea.
DR   HOGENOM; CLU_016922_10_0_2; -.
DR   InParanoid; Q6L0X6; -.
DR   OrthoDB; 6534at2157; -.
DR   Proteomes; UP000000438; 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:AAT43376.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AAT43376.1}.
SQ   SEQUENCE   448 AA;  50239 MW;  ACD11631D76C10CC CRC64;
     MEALKGINIK VEPPGPIAKK IIEMDEKYLA RSTKSLPIVA KRGYNSYIED VDGNVFLDFT
     TGISTTNIGY MNKNVLDAVE EQLHQLWHFA GTDFYYEAQV NAAKALGEVA PGNFNKKVFF
     ANSGAESNEA SLKVAKNYTK KRQFIGFIGA FHGRTMGALA FTASKPVQHS MYFPEMPGVV
     HVPYPNPYRN PFNIDGYENP DELVNRTIDF IEKYTLETYL PADDVAAIMV EPIQGEGGYI
     VPPENFHREL IKLAHENNIL LIMDEVQTGF GRTGYFFASE YFKVEPDIIS VAKSIASGIP
     MGASIFNEKF DFDKEGLHSN TFGGNLLASV ACTATINEIK EKKMLENSRK MGKYLNKRLN
     ELKDKYEEIG DVRGLGLMQA IDFVNDRSRR DFNVGLRDRV IERSFKNGLL LLGAGESAIR
     LIPPLIITEE EIDNAIEIID ESINRELK
//
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