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Database: UniProt
Entry: A0A167HJY0_9FLAO
LinkDB: A0A167HJY0_9FLAO
Original site: A0A167HJY0_9FLAO 
ID   A0A167HJY0_9FLAO        Unreviewed;       401 AA.
AC   A0A167HJY0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:OAB78690.1};
GN   ORFNames=ULVI_08900 {ECO:0000313|EMBL:OAB78690.1};
OS   Cochleicola gelatinilyticus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cochleicola.
OX   NCBI_TaxID=1763537 {ECO:0000313|EMBL:OAB78690.1, ECO:0000313|Proteomes:UP000077013};
RN   [1] {ECO:0000313|EMBL:OAB78690.1, ECO:0000313|Proteomes:UP000077013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0005 {ECO:0000313|EMBL:OAB78690.1,
RC   ECO:0000313|Proteomes:UP000077013};
RA   Shin S.-K., Yi H.;
RT   "Ulvibacter sp. LPB0005, isolated from Thais luteostoma.";
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}.
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:OAB78690.1}.
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DR   EMBL; LRXL01000037; OAB78690.1; -; Genomic_DNA.
DR   RefSeq; WP_068591934.1; NZ_LRXL01000037.1.
DR   AlphaFoldDB; A0A167HJY0; -.
DR   STRING; 1763537.ULVI_08900; -.
DR   OrthoDB; 9803729at2; -.
DR   Proteomes; UP000077013; 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: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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:OAB78690.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077013}.
FT   MOD_RES         204
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   401 AA;  43772 MW;  A3A0347B3DFC434D CRC64;
     MAFNPADNIQ DLQYFGEFGG VNPSISDSST YTFLSAKTMF DTFEGNADGC YLYSRHSTPS
     NLYLGEALAA MEGTETANVA ASGMGAITPT ILQFCQAGDH VVSSRTIYGG TYAFLKNFAP
     RMDIHTSFVD ITKLDVVEAA ITKNTKVLYC ESVSNPLLEV ADIKGLAKIA KKYNLQLLVD
     NTFSPLNISP AKLGADVVLH SLTKFINGSS DTMGGVVCGT QELIDTLRNV NDGASMLLGA
     SMDSMRAASI MKNLRTLHIR IKQHSKNALY LAERFQKEKI KTVYPGLKSH PGHELFKSMM
     NEEYGYGGML TLDVGSLDKA NELMELMQER NLGYLAVSLG FYKTLFSAPG SSTSSEIPEQ
     EQAEMGLSDG LIRFSIGLDN DIERTFNMMR ECMVEVGVLK A
//
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