ID A0A0D8XI47_DICVI Unreviewed; 416 AA.
AC A0A0D8XI47;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Aminotransferase, class III {ECO:0000313|EMBL:KJH43407.1};
GN ORFNames=DICVIV_10584 {ECO:0000313|EMBL:KJH43407.1};
OS Dictyocaulus viviparus (Bovine lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae; Dictyocaulus.
OX NCBI_TaxID=29172 {ECO:0000313|EMBL:KJH43407.1, ECO:0000313|Proteomes:UP000053766};
RN [1] {ECO:0000313|EMBL:KJH43407.1, ECO:0000313|Proteomes:UP000053766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HannoverDv2000 {ECO:0000313|EMBL:KJH43407.1,
RC ECO:0000313|Proteomes:UP000053766};
RA Mitreva M.;
RT "Draft genome of the bovine lungworm Dictyocaulus viviparus.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HannoverDv2000 {ECO:0000313|Proteomes:UP000053766};
RX PubMed=26856411; DOI=10.1038/srep20316;
RA McNulty S.N., Strube C., Rosa B.A., Martin J.C., Tyagi R., Choi Y.J.,
RA Wang Q., Hallsworth Pepin K., Zhang X., Ozersky P., Wilson R.K.,
RA Sternberg P.W., Gasser R.B., Mitreva M.;
RT "Dictyocaulus viviparus genome, variome and transcriptome elucidate
RT lungworm biology and support future intervention.";
RL Sci. Rep. 6:20316-20316(2016).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN716562; KJH43407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D8XI47; -.
DR STRING; 29172.A0A0D8XI47; -.
DR Proteomes; UP000053766; Unassembled WGS sequence.
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; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 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:KJH43407.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000053766};
KW Transferase {ECO:0000313|EMBL:KJH43407.1}.
SQ SEQUENCE 416 AA; 46274 MW; D4958A6218406898 CRC64;
MVSKASMQYL YDEKGMQYLD CISNVQHVGH CHPQVVETIS RQLATSTCNV RFVSQKLTDC
AESLLQTLPG LDTVLFCNSG SEANDLALRL ARDYTKHTDA IVLNHAYHGH VTTTMQLSPY
KFDHGSTITK PEWVHVAPTP DVYRGDYRLA DDELIDTEKL EKAGIYYAET VTNIIEQAEK
NGRTIAAYFA EALQSCGGQV IPPPGYFTEV ARSVRRHGGL VVIDEVQTGF GRVGKKFWAY
QLYDDGFCPD IVTMGKPMGN GFPVSAVVTT RKIANALGGS VGYFNTYGGN PVACAAVLGV
MRVIREEKLL NHSEMMGEEF KKQLNQLKKK YKCIGDIRGV GLFWGIDLVK DRETREPDQK
LALSLILKLR RERGILLNAD GPFTNILKIK PPLCFNMQNL IDTINALDRT LAELGQ
//