ID A0A0R2A6Y0_9LACO Unreviewed; 399 AA.
AC A0A0R2A6Y0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:KRM61220.1};
GN ORFNames=FC26_GL001902 {ECO:0000313|EMBL:KRM61220.1};
OS Paucilactobacillus vaccinostercus DSM 20634.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1423813 {ECO:0000313|EMBL:KRM61220.1, ECO:0000313|Proteomes:UP000051733};
RN [1] {ECO:0000313|EMBL:KRM61220.1, ECO:0000313|Proteomes:UP000051733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20634 {ECO:0000313|EMBL:KRM61220.1,
RC ECO:0000313|Proteomes:UP000051733};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
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:KRM61220.1}.
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DR EMBL; AYYY01000030; KRM61220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2A6Y0; -.
DR STRING; 1423813.FC26_GL001902; -.
DR PATRIC; fig|1423813.3.peg.1931; -.
DR Proteomes; UP000051733; 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 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 Lyase {ECO:0000313|EMBL:KRM61220.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000051733}.
FT MOD_RES 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 399 AA; 43463 MW; 9BEEF5C2E8F0C1E2 CRC64;
MEGLNMTGFN TRLIHGQNIN DNQTGAVNVP VYQSSTYAYP DINGKVRWDY SRSGNPTREY
LEKQIATLEH GANGFAFASG MAAIHAALAI FKEGDHILIG DQIYGGTYRL INDYFQARGI
TFTSVNTQDL EAVKAAIQPN TKAIYFEPVT NPLLQVTSVR AIAAVAKAHD FLTIVDNTFL
TPYLQQPLDL GADIVVHSAT KYLGGHSDVI AGLVVTKTKA LGKRIYFIQN ALGGVLSPEN
ANLVRRGIQT LSVRMDRQQE NARQLIDYLA SRDEVATIHY PGIAGSRDHE IAAEECDGFG
GVFSFELQDD VDAPAFVNSL QLIRLAVSLG AVESLAELPY EMSHAELPPE ERLAAGITPQ
LIRISVGIED AADLISDLNQ ALATATRRQN VHILKRSIG
//
