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Entry: A0A0H5C048_CYBJN
LinkDB: A0A0H5C048_CYBJN
Original site: A0A0H5C048_CYBJN 
ID   A0A0H5C048_CYBJN        Unreviewed;       543 AA.
AC   A0A0H5C048; A0A1E4S9C6;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=PLP-dependent transferase {ECO:0000313|EMBL:ODV76117.1};
DE   SubName: Full=STR2 protein {ECO:0000313|EMBL:CEP20802.1};
GN   Name=STR2 {ECO:0000313|EMBL:CEP20802.1};
GN   ORFNames=BN1211_0756 {ECO:0000313|EMBL:CEP20802.1}, CYBJADRAFT_192864
GN   {ECO:0000313|EMBL:ODV76117.1};
OS   Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617
OS   / NBRC 0987 / NRRL Y-1542) (Torula yeast) (Candida utilis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=983966 {ECO:0000313|EMBL:CEP20802.1, ECO:0000313|Proteomes:UP000038830};
RN   [1] {ECO:0000313|EMBL:CEP20802.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS1600 {ECO:0000313|EMBL:CEP20802.1};
RA   Jaenicke S.;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000038830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC   NRRL Y-1542 {ECO:0000313|Proteomes:UP000038830};
RX   PubMed=26150016; DOI=10.1016/j.jbiotec.2015.06.423;
RA   Rupp O., Brinkrolf K., Buerth C., Kunigo M., Schneider J., Jaenicke S.,
RA   Goesmann A., Puehler A., Jaeger K.-E., Ernst J.F.;
RT   "The structure of the Cyberlindnera jadinii genome and its relation to
RT   Candida utilis analyzed by the occurrence of single nucleotide
RT   polymorphisms.";
RL   J. Biotechnol. 211:20-30(2015).
RN   [3] {ECO:0000313|EMBL:ODV76117.1, ECO:0000313|Proteomes:UP000094389}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC   NRRL Y-1542 {ECO:0000313|Proteomes:UP000094389}, and NRRL Y-1542
RC   {ECO:0000313|EMBL:ODV76117.1};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; CDQK01000001; CEP20802.1; -; Genomic_DNA.
DR   EMBL; KV453925; ODV76117.1; -; Genomic_DNA.
DR   RefSeq; XP_020073156.1; XM_020217458.1.
DR   STRING; 983966.A0A0H5C048; -.
DR   GeneID; 30991854; -.
DR   OMA; HYQELDE; -.
DR   OrthoDB; 35837at2759; -.
DR   Proteomes; UP000038830; Unassembled WGS sequence.
DR   Proteomes; UP000094389; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42699; -; 1.
DR   PANTHER; PTHR42699:SF1; CYSTATHIONINE GAMMA-SYNTHASE-RELATED; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU362118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094389};
KW   Transferase {ECO:0000313|EMBL:ODV76117.1}.
SQ   SEQUENCE   543 AA;  61588 MW;  FBFDAE393BF0E520 CRC64;
     MEAPSQEIGE SIPNNTPHAV SVTLPTWEAT VGYERGEDWV VQRMKLGYPR FFIHSKIKEL
     CALVEEKFGR EGERAFVFPS YAVAKRCREF VKEKTSNAPL PTIRILQLST PPPRSKEEES
     YRKEAHIAAV FVPESEFVLA KNYWQHSGEG ISSRLGEYVL QELKIVDNNL QEDKDKEYKV
     FIEERFGRNL DLGFTSEAKT ALRRRIAGVM DEASPVAGRV DEDDVFLYPS GMAAIFNAHL
     CLLKTLPNEK SVCFGFPYVD TLNILKKFGP GVHFYGFGDD DSLDELEAKL SQGEKILGLF
     CECPSNPLLK TPNLKRIHQL SLTYKFPVVV DETVGNFLNI DVRPYTDIIV SSLTKVFSGD
     SNVMAGSLVI NPASQFYPLF QQYFRQNYED IFWAEDAIYL ERNSRDFESR SHKVNVNSEA
     VVDLFQKCPI ITQVFYPKVN DSRKYYEDIK TPNGGYGGLI SIVFQKQEQA VAFFDSLELS
     KGPSLGTNFT LVCPYAILAH YQELDEVEKW GIDRNLVRLS IGLEDQDALL QTMQMALNLA
     IQA
//
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