ID A0A0S1S8V7_9FLAO Unreviewed; 392 AA.
AC A0A0S1S8V7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ALM06863.1};
GN ORFNames=SB49_02870 {ECO:0000313|EMBL:ALM06863.1};
OS Sediminicola sp. YIK13.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Sediminicola.
OX NCBI_TaxID=1453352 {ECO:0000313|EMBL:ALM06863.1, ECO:0000313|Proteomes:UP000063759};
RN [1] {ECO:0000313|Proteomes:UP000063759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIK13 {ECO:0000313|Proteomes:UP000063759};
RA Kwon Y.M., Kim S.-J.;
RT "Genome sequence of Sediminicola sp. YIK13.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALM06863.1, ECO:0000313|Proteomes:UP000063759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIK13 {ECO:0000313|EMBL:ALM06863.1,
RC ECO:0000313|Proteomes:UP000063759};
RX PubMed=26823585;
RA Kwon Y.M., Kim S.J.;
RT "Complete Genome Sequence of the Proteorhodopsin-Containing Marine
RT Bacterium Sediminicola sp. YIK13.";
RL Genome Announc. 4:e01635-15(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}.
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DR EMBL; CP010535; ALM06863.1; -; Genomic_DNA.
DR RefSeq; WP_062053669.1; NZ_CP010535.1.
DR AlphaFoldDB; A0A0S1S8V7; -.
DR STRING; 1453352.SB49_02870; -.
DR KEGG; syi:SB49_02870; -.
DR PATRIC; fig|1453352.4.peg.598; -.
DR OrthoDB; 9803729at2; -.
DR Proteomes; UP000063759; 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:SF90; 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:ALM06863.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000063759}.
FT MOD_RES 199
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 392 AA; 43060 MW; 835ED087305895B5 CRC64;
MADNIKGLNT ICTHFGEIQD EQFKGAVSPL FMSTSYAFED VDVKRYPRYF NTPNQVALSK
KIAALEHAEA AIIFGSGMAA ISTALMAFLK AGDHIVLQNT LYGGTYNLVT EEFHKFGIEY
SFTTGLEPAD FEAKIKENTK VIYIETPSNP LLTITDLEAV AQIAKKHGLV SMIDNTFASP
VNQNPIDFGI DVVLHSATKY MGGHSDILAG AVASSHEHME RIFQLAKNFG GSLSDYTVWL
LERSIKTMGI RVRAQNENAM EMAKYLYVHH DLQAVFYPGL ESHPGHELAK AQMKGFGGML
SFELNKDLNS SLFQKSLRLI KSSMSLAGVE STVLSPTLTS HSLLSAEERE KQGIADGLIR
FSVGIEEVED LIADIEQALA TVKAKSRTVH SN
//
