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Database: UniProt
Entry: A0A0N5DZR0_TRIMR
LinkDB: A0A0N5DZR0_TRIMR
Original site: A0A0N5DZR0_TRIMR 
ID   A0A0N5DZR0_TRIMR        Unreviewed;       396 AA.
AC   A0A0N5DZR0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   10-OCT-2018, entry version 13.
DE   RecName: Full=Serine--pyruvate aminotransferase {ECO:0000256|PIRNR:PIRNR000524};
DE            EC=2.6.1.44 {ECO:0000256|PIRNR:PIRNR000524};
DE            EC=2.6.1.51 {ECO:0000256|PIRNR:PIRNR000524};
DE   AltName: Full=Alanine--glyoxylate aminotransferase {ECO:0000256|PIRNR:PIRNR000524};
OS   Trichuris muris (Mouse whipworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=70415 {ECO:0000313|Proteomes:UP000046395, ECO:0000313|WBParaSite:TMUE_s0117003500};
RN   [1] {ECO:0000313|Proteomes:UP000046395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Edinburgh {ECO:0000313|Proteomes:UP000046395};
RA   Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D.,
RA   Schwartz K.J., Yoon K.;
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000046395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Edinburgh {ECO:0000313|Proteomes:UP000046395};
RA   Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA   Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA   Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT   "The whipworm genome and dual-species transcriptomics of an intimate
RT   host-pathogen interaction.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|WBParaSite:TMUE_s0117003500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Edinburgh {ECO:0000313|WBParaSite:TMUE_s0117003500};
RG   Helminth Genomes Consortium;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|WBParaSite:TMUE_s0117003500}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: L-alanine + glyoxylate = pyruvate + glycine.
CC       {ECO:0000256|PIRNR:PIRNR000524}.
CC   -!- CATALYTIC ACTIVITY: L-serine + pyruvate = 3-hydroxypyruvate + L-
CC       alanine. {ECO:0000256|PIRNR:PIRNR000524}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000524,
CC         ECO:0000256|PIRSR:PIRSR000524-50,
CC         ECO:0000256|RuleBase:RU004504};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|PIRNR:PIRNR000524,
CC       ECO:0000256|RuleBase:RU004075}.
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DR   WBParaSite; TMUE_s0117003500; TMUE_s0117003500; TMUE_s0117003500.
DR   Proteomes; UP000046395; Unassembled WGS sequence.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004760; F:serine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000046395};
KW   Pyridoxal phosphate {ECO:0000256|PIRNR:PIRNR000524,
KW   ECO:0000256|PIRSR:PIRSR000524-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000046395}.
FT   DOMAIN       55    385       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   MOD_RES     219    219       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR000524-50}.
SQ   SEQUENCE   396 AA;  44327 MW;  8790E0E22650CC61 CRC64;
     MTLKMTRALR SQPRTTHVLP PKALLQPSDI RERYLFGPGP TNLLPRAQKG LTMPMTGYLH
     PHFTQIMDDV KAGLQYMFQT RNRFTMAVTG SGHAAMEACL VNLLEHNEKL LVLEHGMWGE
     RAVEMGLRMG LRVNKICRPP GEVFTFDEIR QAVEIYEPRV LFVCHGESST GALQPLDGLG
     ELCSRHDCLL LVDMVMSLGA ATASVDVMGI DCAYSASQKV LSCPAGLAPV TLNDRAMKRI
     FHRKTSPASF YLDLALIGNY WGCFDENRRY HHTACMPLVY ALRESLSNAV QEGLENIVER
     HQRNAAELCT RLKNLGFRML VSDQDVRLPS LTGINVLPGQ DWKQFIQHLF TEHNIEIAGG
     LGATVGRIFR IGLMGHNSTR ENIDRILQAF EASIKK
//
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