ID J4H380_9APHY Unreviewed; 495 AA.
AC J4H380;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Acetylornithine transaminase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FIBRA_04921 {ECO:0000313|EMBL:CCM02809.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM02809.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM02809.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM02809.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
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; HE797094; CCM02809.1; -; Genomic_DNA.
DR RefSeq; XP_012182092.1; XM_012326702.1.
DR AlphaFoldDB; J4H380; -.
DR STRING; 599839.J4H380; -.
DR GeneID; 24097720; -.
DR HOGENOM; CLU_016922_10_1_1; -.
DR InParanoid; J4H380; -.
DR OrthoDB; 5487467at2759; -.
DR Proteomes; UP000006352; 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:UP000006352};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT REGION 31..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 52592 MW; 98F904F4A6E24932 CRC64;
MRGPAGSTGR TLTRHGRKYR GVRLASSLTE NAPRAAPKLP AKPSTRYTSV THAEDTTSIS
AGVKALLDRS NAYILPVYAR PPFVLSHGKG AYVWDTEGRR YLDFSAGIAV NALGHADQGV
ANVLASEAAT LLHTSNAYHH KWAGKLAELL VTLTQREGGL GWEGGSTHSS SSGSSGAKVF
FSNSGTEANE GALKIARKLG KARWAAATGK EWDDPSCDKH EIVCFESAFH GRSMGALSVT
TNAKYQKPFT PLIPGIRVGK LNAADDLERL VGEKTCAVIV EPIQGEGGIH PAEVKWLQAL
RKKCDEVGAV LIYDEIQCGL YRTGDLWAHS TLPVDAHPDI VTMAKPLANG YPIGAVLMRD
HVAETMTAGT HGTTFGGSPL ACALGYYVLS RVSERPFVAN IAETSAYLHD RLSQLPGWFP
DILQPGVRGR GLILGLGFRD GTHPAKLVGM ARERGVLLLT AGADAVRLVP SLNIGQAEVD
VAVDVIESCL GHGVA
//
