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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//