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Database: UniProt
Entry: I9C177_9SPHN
LinkDB: I9C177_9SPHN
Original site: I9C177_9SPHN 
ID   I9C177_9SPHN            Unreviewed;       390 AA.
AC   I9C177;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:EIZ77235.1};
GN   ORFNames=WSK_4227 {ECO:0000313|EMBL:EIZ77235.1};
OS   Novosphingobium sp. Rr 2-17.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=555793 {ECO:0000313|EMBL:EIZ77235.1, ECO:0000313|Proteomes:UP000004732};
RN   [1] {ECO:0000313|EMBL:EIZ77235.1, ECO:0000313|Proteomes:UP000004732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RR2-17 {ECO:0000313|Proteomes:UP000004732};
RX   PubMed=22933764; DOI=10.1128/JB.01159-12;
RA   Gan H.M., Chew T.H., Hudson A.O., Savka M.A.;
RT   "Genome Sequence of Novosphingobium sp. Strain Rr 2-17, a Nopaline Crown
RT   Gall-Associated Bacterium Isolated from Vitis vinifera L. Grapevine.";
RL   J. Bacteriol. 194:5137-5138(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC         Evidence={ECO:0000256|ARBA:ARBA00001535};
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|ARBA:ARBA00009077, 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:EIZ77235.1}.
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DR   EMBL; AKFJ01000150; EIZ77235.1; -; Genomic_DNA.
DR   AlphaFoldDB; I9C177; -.
DR   PATRIC; fig|555793.3.peg.4146; -.
DR   eggNOG; COG0626; Bacteria.
DR   Proteomes; UP000004732; 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: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; IPR006233; Cys_b_lyase_bac.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01324; cysta_beta_ly_B; 1.
DR   PANTHER; PTHR43500; CYSTATHIONINE BETA-LYASE-RELATED; 1.
DR   PANTHER; PTHR43500:SF1; CYSTATHIONINE BETA-LYASE-RELATED; 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:EIZ77235.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004732}.
FT   MOD_RES         206
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   390 AA;  41751 MW;  B9C0A8107F0490C3 CRC64;
     MKFDDLPSGE ATRMIHPAPD GDIVLRTAAP VLQRGTTVLL DSCEAFGRKS PTYGRSGLAT
     QAELRRSLCT LEQGEVAELY PSGLAALSGA ILAVCRAGDE ILICDTIYGP TRRFAESTMA
     DYGVTTRYFP ADIALDELEG LIGPSTRLIV LESPGSLTLD MMDIPALAAL ARSRGVLTLV
     DNTYAAGVLF KPLDHGIDIS VQALTKYVCG HSDVFMGCAV ARGEVGEMLK RSSRSVGWAV
     SSDDAYLALR GLRTLHARLA RHGESALEVA TWLAAQPQVS EVLCPALPGS RGHEVFKRDY
     LGGNGLVTIV LDAPESAATA FLDALRIFGL GFSWGGFESL AIPCNDQLRQ RRFAPALEQP
     VIRLHVGLEN TADLIAELRT ALTARAEARI
//
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