ID   B1YD35_PYRNV            Unreviewed;       446 AA.
AC   B1YD35;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ACB39698.1};
GN   OrderedLocusNames=Tneu_0759 {ECO:0000313|EMBL:ACB39698.1};
OS   Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 /
OS   V24Sta) (Thermoproteus neutrophilus).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=444157 {ECO:0000313|EMBL:ACB39698.1, ECO:0000313|Proteomes:UP000001694};
RN   [1] {ECO:0000313|EMBL:ACB39698.1, ECO:0000313|Proteomes:UP000001694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta
RC   {ECO:0000313|Proteomes:UP000001694};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL   Submitted (MAR-2008) 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; CP001014; ACB39698.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1YD35; -.
DR   STRING; 444157.Tneu_0759; -.
DR   KEGG; tne:Tneu_0759; -.
DR   eggNOG; arCOG00915; Archaea.
DR   HOGENOM; CLU_016922_10_0_2; -.
DR   OrthoDB; 6534at2157; -.
DR   Proteomes; UP000001694; 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:ACB39698.1};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ACB39698.1}.
SQ   SEQUENCE   446 AA;  49044 MW;  18CE724128DCCB4F CRC64;
     MPKWHWPIDP DAVPRILVEP PGPRALEVVR RDGEVIMQSF SRWYPLVVAR GYGPVVEDVD
     GNLYIDYNAG IAVANVGHAH PKVVEAIKRQ AELFLHYSLT DFYYEVAVKL AERLIAIAPI
     SGRKKVFFTN SGTESIEGVL KIARGYFKGQ RPYVIAFLGA FHGRTYGSMS LTASKPVHRR
     HFSPMVPNVI HAPFPHPVHC PFKAETPEEC GEYALAFLED WIFRRLVDPS EVALVLMEPV
     QGEGGYVVPP RNFVQGLRKM TYEHGILFAV DEVQTGFGRT GRWFAVEHFG VEPDLIATAK
     AIAAGLPLGA IIGRAEVMSL PRGAHANTFG GNPVAAAAAL ASLEVIEEEG LLNHAETLGE
     ELKKLFRDEV GHRHDVRGLG LMIGIELLEG KKPAKYLEDV LLKAFKRGVA VIGAGLSTVR
     IAPPLVIPRD MAFKAAEIIL DVLRGH
//