ID F4HI77_PYRSN Unreviewed; 443 AA.
AC F4HI77;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AEC51004.1};
GN OrderedLocusNames=PNA2_0086 {ECO:0000313|EMBL:AEC51004.1};
OS Pyrococcus sp. (strain NA2).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=342949 {ECO:0000313|EMBL:AEC51004.1, ECO:0000313|Proteomes:UP000008293};
RN [1] {ECO:0000313|EMBL:AEC51004.1, ECO:0000313|Proteomes:UP000008293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA2 {ECO:0000313|EMBL:AEC51004.1,
RC ECO:0000313|Proteomes:UP000008293};
RX PubMed=21602357; DOI=10.1128/JB.05150-11;
RA Lee H.S., Bae S.S., Kim M.S., Kwon K.K., Kang S.G., Lee J.H.;
RT "Complete genome sequence of hyperthermophilic Pyrococcus sp. strain NA2,
RT isolated from a deep-sea hydrothermal vent area.";
RL J. Bacteriol. 193:3666-3667(2011).
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; CP002670; AEC51004.1; -; Genomic_DNA.
DR RefSeq; WP_013747562.1; NC_015474.1.
DR AlphaFoldDB; F4HI77; -.
DR STRING; 342949.PNA2_0086; -.
DR GeneID; 10553542; -.
DR KEGG; pyn:PNA2_0086; -.
DR PATRIC; fig|342949.8.peg.86; -.
DR eggNOG; arCOG00916; Archaea.
DR HOGENOM; CLU_016922_10_0_2; -.
DR OrthoDB; 6534at2157; -.
DR Proteomes; UP000008293; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:AEC51004.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AEC51004.1}.
SQ SEQUENCE 443 AA; 49483 MW; 05F77DF994CEFD39 CRC64;
MDPWEVVERY SKVIAPANRT TYFPLVPVRA ENAKVWDVNG REYIDFLSDA AVQNVGHNNP
RVIKAVEEQI KRLMHATFIY AFPLEPLLLA EKLVEIVPIE NAKVAFGLSG SDANDGAIKF
ARAYTERQII LSYIRSFYGA TYGSMSITGL DPKVKAMVGE LSGVHFIPYP NCYRCPFGKD
PKTCNMECVE YIKEKFEGEI YADGVAALFA EPIQGDAGMV VPPKDYFKKV KRILDDHGIL
LVVDEIQSGF GRTGRWFAIE HFGVEPDIIT VAKPLGGGLP ISAIIGRSEI MDSLPPLSHA
FTLSGNPTAA KAALAVIEEI EEKNLLKRAE RLGEHAMKRL RGMMRRHELI GDVRGLGLMI
GVELVKDRET KERAYEETKK VVWRAFELGL IVTFLQGNVL RIQPPLTIEE ELLDEGLDRL
KEAIEDVEEG KVPDSVLDKV QGW
//
