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
//