ID A0A067NAR8_PLEOS Unreviewed; 464 AA.
AC A0A067NAR8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Acetylornithine aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PLEOSDRAFT_1078885 {ECO:0000313|EMBL:KDQ24929.1};
OS Pleurotus ostreatus PC15.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ24929.1, ECO:0000313|Proteomes:UP000027073};
RN [1] {ECO:0000313|Proteomes:UP000027073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; KL198011; KDQ24929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067NAR8; -.
DR STRING; 1137138.A0A067NAR8; -.
DR HOGENOM; CLU_016922_10_0_1; -.
DR InParanoid; A0A067NAR8; -.
DR OrthoDB; 345661at2759; -.
DR Proteomes; UP000027073; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; 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:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 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:0000256|ARBA:ARBA00022576};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000027073};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ SEQUENCE 464 AA; 50298 MW; AFA00EF629C60171 CRC64;
MLRNAIRAQG RILTRGVATS ASSAELLDIG ERHVTKGLGR LVKGIMKKGE GSYVFMDDGR
RLLDFTCGIG VANLGHCHPK ISKAAADQCM SIVHAQCSIA FHEPYLRLIQ KLLPIMPHPS
LDSFFFWNSG SEAVEAALKM ARTFTGRQNI IAMQGAYHGR TYGAMAVTKS KTIYSQGTMP
LMPGVFTTPF PYWHHHNVHP STPTSELTRD ALYQLDLLLS QQTHPKDTAA ILIEPVIGEG
GYVPAPAEYL QGLRAICDKH GIMLIIDEVQ SGFGRTAGSG FFAIQDAGVR PDILVIAKGL
ANGFPLSGIV TQKQWTDKLL PGSMGGTYAG NAVSCAAACA VADAMHEEQT LENVRARSPQ
LVSFLNGVKA KYPEYILDVR GKGLMIAMEF ASPTVSKHDV ARNEKAPEKV AAKITAKCLE
KGMLLLTTSV YETIRFIPPL NITEADLQKG CQIFESAVKE VLEG
//
