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Database: UniProt
Entry: A0A0R2ADA2_9LACO
LinkDB: A0A0R2ADA2_9LACO
Original site: A0A0R2ADA2_9LACO 
ID   A0A0R2ADA2_9LACO        Unreviewed;       313 AA.
AC   A0A0R2ADA2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Cysteine synthase {ECO:0000313|EMBL:KRM65393.1};
GN   ORFNames=FC14_GL001361 {ECO:0000313|EMBL:KRM65393.1};
OS   Ligilactobacillus agilis DSM 20509.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1423718 {ECO:0000313|EMBL:KRM65393.1, ECO:0000313|Proteomes:UP000051008};
RN   [1] {ECO:0000313|EMBL:KRM65393.1, ECO:0000313|Proteomes:UP000051008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20509 {ECO:0000313|EMBL:KRM65393.1,
RC   ECO:0000313|Proteomes:UP000051008};
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   -!- 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:KRM65393.1}.
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DR   EMBL; AYYP01000015; KRM65393.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2ADA2; -.
DR   PATRIC; fig|1423718.3.peg.1422; -.
DR   Proteomes; UP000051008; Unassembled WGS sequence.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProt.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   CDD; cd01561; CBS_like; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF242; O-ACETYLSERINE DEPENDENT CYSTATHIONINE BETA-SYNTHASE; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051008}.
FT   DOMAIN          20..300
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   313 AA;  33291 MW;  BA672B573843E836 CRC64;
     MSVFFAFLEV NEMLVTSVYQ LVGQTPLLEL PAPNESRIYA KLEMFNPGGS IKDRLGLALV
     RGALEAGVIN RQTTIIEPTA GNTGIGLALA ASKYQLRLIL VVPAGFSQEK QVLMKALGAE
     LVLSDPALGM QGALAKSRQL ASQIANSYVF NQFENVANPK AYRLLAKEIK QDLGKLTPTA
     FVAGAGTGGT FAGTLQELRQ VYPDIKGIVV QPAGSILSGG VAHQHKTEGI GVEIEPPFFK
     DLGIDGIATI SDEAAFKQVR QAASKWGLLI GSSSGAALQA SLELAAKLPA RSKIVTIFPD
     SSERYLSKNI YNF
//
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