ID A0A126P709_9BACT Unreviewed; 384 AA.
AC A0A126P709;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:AMJ64678.1};
GN ORFNames=AXW84_03970 {ECO:0000313|EMBL:AMJ64678.1};
OS Hymenobacter sp. PAMC 26628.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1484118 {ECO:0000313|EMBL:AMJ64678.1, ECO:0000313|Proteomes:UP000059956};
RN [1] {ECO:0000313|EMBL:AMJ64678.1, ECO:0000313|Proteomes:UP000059956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC26628 {ECO:0000313|EMBL:AMJ64678.1,
RC ECO:0000313|Proteomes:UP000059956};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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; CP014304; AMJ64678.1; -; Genomic_DNA.
DR RefSeq; WP_068228996.1; NZ_CP014304.1.
DR AlphaFoldDB; A0A126P709; -.
DR STRING; 1484118.AXW84_03970; -.
DR KEGG; hyz:AXW84_03970; -.
DR OrthoDB; 634606at2; -.
DR Proteomes; UP000059956; Chromosome.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF15; CYSTATHIONINE GAMMA-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:AMJ64678.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000059956}.
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 384 AA; 40328 MW; 524015AA90C7006A CRC64;
MNLTNIHPKV TPIYQTSVFK FASLAELEEY YTAPGRGGRY GYSRSEHPNT EELVAAVAQL
EGVAGGALAG VATGAGLSGL LAAVLATCQA GDHVLCPAEL YGGSVVLLSN ELSRLGIETS
YVPLADLYDL ARHARPNTKL VLAETLSNPL LTVLDGPRLA AACRAQGVLL LIDNTFASPA
ISQPFSWGAD LVWHSATKYL GGHSDVTAGL VLARDPAVAQ RLRQVGGSLG LTLAPLESWL
TLRGTKTLRL RMRQHSENAL AVAQFLAQQP AVGQVFYPGL PTDPGHALAA AQLRGGQFGG
MLSFRLADDT AAAADAFIQK SQLFPLAPSL AGVDSSCSYP LATSHRHIPD ERRRALGITP
GLIRLSVGIE EASDLLADLA QALG
//
