ID A0A167EY67_9HYPO Unreviewed; 424 AA.
AC A0A167EY67;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:OAA44561.1};
GN ORFNames=BBO_04044 {ECO:0000313|EMBL:OAA44561.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA44561.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA44561.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA44561.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA44561.1}.
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DR EMBL; AZHA01000010; OAA44561.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167EY67; -.
DR OrthoDB; 5482552at2759; -.
DR Proteomes; UP000076863; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; PTHR11808:SF35; CYSTATHIONINE GAMMA-SYNTHASE (AFU_ORTHOLOGUE AFUA_7G01590); 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:OAA44561.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 424 AA; 46265 MW; BCB831887781082F CRC64;
MSEQAQEDHG PSLALRPSSK HTRISEQAQE DSGLSLASRL VHGDDGISTH RAVAPAMHVS
TTFRYNDNPD MLEPEVYVNP DAPLDSHVYS RYTSPNTTRL EAILTSVLGG KALTYASGLS
AFHMMLVRIN PKRIAIGDGY HGCHGIIGIQ SRLTGLQKLP LDCDPSELQP GDIIHVETPL
NPTGEARDLQ YYADKAHAVG AYLTVDATFA PPPLQDPFAH GADLVMHSGT KYFGGHSDML
CGVLALSPRL PFDDWYPAMV CDRAILGCVM GSMEGWLGLR SMRTMELRVL RQSKTATDLV
SWLAAQVKDP ESPVAKVVDH VKHASLQPEA ADESSWLRRQ MPGGYGPVFA LAMKSEAVAK
RLPSKLRLFH HATSLGGVES LIEWRAMTDK TVARNLLRVS IGVEALEDLK ADFEQAFAKL
AVEV
//
