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Database: UniProt
Entry: C9SJ68_VERA1
LinkDB: C9SJ68_VERA1
Original site: C9SJ68_VERA1 
ID   C9SJ68_VERA1            Unreviewed;       441 AA.
AC   C9SJ68;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   13-SEP-2023, entry version 65.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:EEY18230.1};
GN   ORFNames=VDBG_04339 {ECO:0000313|EMBL:EEY18230.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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; DS985218; EEY18230.1; -; Genomic_DNA.
DR   RefSeq; XP_003004733.1; XM_003004687.1.
DR   AlphaFoldDB; C9SJ68; -.
DR   STRING; 526221.C9SJ68; -.
DR   GeneID; 9536704; -.
DR   KEGG; val:VDBG_04339; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   HOGENOM; CLU_018986_2_1_1; -.
DR   OMA; MPIYQTA; -.
DR   OrthoDB; 6018at2759; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR006238; Cys_b_lyase_euk.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01329; cysta_beta_ly_E; 1.
DR   PANTHER; PTHR11808:SF50; CYSTATHIONINE BETA-LYASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:EEY18230.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         242
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   441 AA;  47511 MW;  C951259B1685DB25 CRC64;
     MAAQSSFSGG NGGPSKPSEL SKRLDLDGHD LPPSPAPSSP RNGRRRYALA TELVYTETND
     QYGSSSIPIY QSATFKQSSA RGGNSEYDYT RSGNPTRTHL ERHMAKIMNA SRALAVGSGM
     GALDVITRLL RPGDEVITGD DLYGGTNRLL AYLSSNQGIV VHHVNTTTVD AVRDVVSDKT
     AMVLLETPTN PLIKVIDIPS IARVVHEVND KALVVVDNTM LSPMLCNPLD LGADIVYESG
     TKYLSGHHDI MAGIIGVNDA AVADKLYFTI NASGCGLSPN DSFLLMRGVK TLAIRMEKQQ
     SNAQQIAEFL ENHGFRVRYP GLKSHPQYDL HWSMARGAGA VLSFETGDAS LSERIVEAAR
     LWGISVSFGC VNSLISMPCQ MSHASIDAKT RKERQMPEDI IRLCVGIEDV EDLIDDLSRA
     LVQAGAVTVT LEGIQANPVA A
//
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