ID   A1RVB2_PYRIL            Unreviewed;       447 AA.
AC   A1RVB2;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=4-aminobutyrate aminotransferase apoenzyme {ECO:0000313|EMBL:ABL88894.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABL88894.1};
GN   OrderedLocusNames=Pisl_1743 {ECO:0000313|EMBL:ABL88894.1};
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=384616 {ECO:0000313|EMBL:ABL88894.1, ECO:0000313|Proteomes:UP000002595};
RN   [1] {ECO:0000313|Proteomes:UP000002595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189 / GEO3 {ECO:0000313|Proteomes:UP000002595};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000504; ABL88894.1; -; Genomic_DNA.
DR   RefSeq; WP_011763469.1; NC_008701.1.
DR   AlphaFoldDB; A1RVB2; -.
DR   STRING; 384616.Pisl_1743; -.
DR   GeneID; 4617079; -.
DR   KEGG; pis:Pisl_1743; -.
DR   eggNOG; arCOG00915; Archaea.
DR   HOGENOM; CLU_016922_10_0_2; -.
DR   OrthoDB; 6534at2157; -.
DR   Proteomes; UP000002595; 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:ABL88894.1};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ABL88894.1}.
SQ   SEQUENCE   447 AA;  49322 MW;  35D050B0C3285473 CRC64;
     MPQWHWPIDP DKVPRIVVEP PGPRALSIIK RDEEVLMQSF TRWYPLVVAR GYGPVVEDVD
     GNLYIDYNAG IAVANVGHAH PKVVEAIKRQ AELFLHYSLT DFYYEVAVKL AERLISIAPI
     SGRKKVFFTN SGTESIEGVL KIARGYFKGQ RPYVIAFLGA FHGRTYGSMS LTASKPVHRR
     HFSPMVPNVI HAPFPHPVHC PFKAETPEEC GEYALAFLED WIFRRLVDPS EVALVLIEPV
     QGEGGYVVPP RNFVQGLRKM TQEHGILFAV DEVQTGFGRT GKWFAVEHFG VEPDLIATAK
     AIAAGLPLGA IIGRAEVMSL PRGAHANTFG GNPVAAAAAL ASLEVIEEEG LLNHAETLGE
     ELKKLFRDEV GHRHDVRGLG LMIGIELLDE KKKPAKYLEE VLIKAFKRGV AVIGAGLSTV
     RIAPPLVIPR DMAFKAAEII LDVLRSY
//