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Database: UniProt
Entry: A4ARD6_MARSH
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ID   A4ARD6_MARSH            Unreviewed;       391 AA.
AC   A4ARD6;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:EAR01159.1};
GN   OrderedLocusNames=FB2170_10581 {ECO:0000313|EMBL:EAR01159.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR01159.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR01159.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the genus
RT   Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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; CP002157; EAR01159.1; -; Genomic_DNA.
DR   RefSeq; WP_013306755.1; NC_014472.1.
DR   AlphaFoldDB; A4ARD6; -.
DR   STRING; 313603.FB2170_10581; -.
DR   KEGG; fbc:FB2170_10581; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_0_10; -.
DR   OrthoDB; 9803729at2; -.
DR   Proteomes; UP000001602; Chromosome.
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   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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:EAR01159.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602}.
FT   MOD_RES         199
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   391 AA;  42709 MW;  7D1CC0B48AAC6008 CRC64;
     MGKSNKGVNT ICTHVGEIHD EQFKGAISPL YMSTSYAFED VDVKRYPRYF NTPNQVALSQ
     KIAALEHAEA AMIFGSGMAA ISTALLAFLQ AGDHIVLQKA LYGGTYNFVN EEFSKYGIEF
     SFTEGLEPQD FESKIKDNTK VIFVETPSNP LLTITDLAAI GKIAKKHGLV SMIDNTFASP
     VNQNPLDFGI EIVIHSATKY MGGHSDICAG AVASTAENME RIFHLAKNLG GSLSDYTVWL
     LERSIKTMGI RVKAQNANAQ YLAEYLDAHQ EIDRVYYPGL PNHPGHDLAK AQMKGFGGMM
     SFELDKSYDA SEFQKALSLI KPSMSLAGVE STVLSPTLAS HALMSPEERK NQGIADGLIR
     FSVGIEEAED LIADIEQALE KVRNSSMVST D
//
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