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}.
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; 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
//