ID B3DT90_BIFLD Unreviewed; 394 AA.
AC B3DT90;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Cystathionine beta-lyases/cystathionine gamma-synthase {ECO:0000313|EMBL:ACD98359.1};
GN Name=metC3 {ECO:0000313|EMBL:ACD98359.1};
GN OrderedLocusNames=BLD_0913 {ECO:0000313|EMBL:ACD98359.1};
OS Bifidobacterium longum (strain DJO10A).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=205913 {ECO:0000313|EMBL:ACD98359.1, ECO:0000313|Proteomes:UP000002419};
RN [1] {ECO:0000313|EMBL:ACD98359.1, ECO:0000313|Proteomes:UP000002419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJO10A {ECO:0000313|EMBL:ACD98359.1,
RC ECO:0000313|Proteomes:UP000002419};
RX PubMed=16391088; DOI=10.1128/AEM.72.1.527-535.2006;
RA Lee J.H., O'Sullivan D.J.;
RT "Sequence analysis of two cryptic plasmids from Bifidobacterium longum
RT DJO10A and construction of a shuttle cloning vector.";
RL Appl. Environ. Microbiol. 72:527-535(2006).
RN [2] {ECO:0000313|EMBL:ACD98359.1, ECO:0000313|Proteomes:UP000002419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJO10A {ECO:0000313|EMBL:ACD98359.1,
RC ECO:0000313|Proteomes:UP000002419};
RX PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT reveals loci susceptible to deletion during pure culture growth.";
RL BMC Genomics 9:247-247(2008).
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}.
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DR EMBL; CP000605; ACD98359.1; -; Genomic_DNA.
DR RefSeq; WP_010081119.1; NZ_AABM02000006.1.
DR AlphaFoldDB; B3DT90; -.
DR KEGG; blj:BLD_0913; -.
DR HOGENOM; CLU_018986_2_0_11; -.
DR Proteomes; UP000002419; 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:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 394 AA; 41919 MW; 334C3C0468A57EDF CRC64;
MSAEYNAKFA NTDIATRAIH AGQEPDPTTG AVVTPIFATS TFKQDGVLGL RGGHDYSRSI
NPTRTSFDEQ LAAVEGGKYA LSFSSGLAAI DVLLRSTIKP GDNILLGNDV YGGTYRLLSK
VFVPWGVGLD VVDITDLKAV ETALASKHYQ YVWVETPSNP LLNITDIAAT TEVAHKYGTK
VAVDNTFASP ALQHPLADGA DVVVYSTTKY IGGHSDVVGG AVVVNDEETR EKVAFLQNAA
GAVPSPFDSW LDIRGLKTLD LRVKRHSANA LKVAEWLESQ PSDVIERVWY PGLESHPGHE
IAARQMHGGF GGIVSVQLAA GAEAAKHFVD HTQIFTLAES LGGVESLIEV PAAMTHASVA
GTTLQVPANL VRISVGIENA DDLIADLKQA LDRI
//
