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Database: UniProt
Entry: A0A0T6A1Y7_9BACT
LinkDB: A0A0T6A1Y7_9BACT
Original site: A0A0T6A1Y7_9BACT 
ID   A0A0T6A1Y7_9BACT        Unreviewed;       420 AA.
AC   A0A0T6A1Y7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Pyridoxal-phosphate (PLP) dependent enzyme family {ECO:0000313|EMBL:KRT69075.1};
DE            EC=2.5.1.47 {ECO:0000313|EMBL:KRT69075.1};
GN   Name=cysK {ECO:0000313|EMBL:KRT69075.1};
GN   ORFNames=XU15_C0013G0021 {ECO:0000313|EMBL:KRT69075.1};
OS   candidate division NC10 bacterium CSP1-5.
OC   Bacteria; candidate division NC10.
OX   NCBI_TaxID=1640516 {ECO:0000313|EMBL:KRT69075.1, ECO:0000313|Proteomes:UP000051123};
RN   [1] {ECO:0000313|EMBL:KRT69075.1, ECO:0000313|Proteomes:UP000051123}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-5 {ECO:0000313|EMBL:KRT69075.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated with
RT   bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRT69075.1}.
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DR   EMBL; LDXR01000013; KRT69075.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6A1Y7; -.
DR   STRING; 1640516.XU15_C0013G0021; -.
DR   PATRIC; fig|1640516.3.peg.2009; -.
DR   Proteomes; UP000051123; Unassembled WGS sequence.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd01561; CBS_like; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR   InterPro; IPR003749; ThiS/MoaD-like.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF255; O-PHOSPHOSERINE SULFHYDRYLASE; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF02597; ThiS; 1.
DR   SUPFAM; SSF54285; MoaD/ThiS; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000313|EMBL:KRT69075.1}.
FT   DOMAIN          117..392
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   420 AA;  46313 MW;  C7B705067DAAFB0A CRC64;
     MSVQVRVPQI FRRHTGGAKT VVVEGMTVRD ILENLDKAHP GLRDRLLDGK ELHRFVNIYR
     NDEDIRFLKF LDTEVQEGDV ISILPAVAGG VRVPTRKKAI GGRKTAGGPR PAADTVDAIG
     NTPLVEVQRI SPKSSVRIFC KLEFYNPTGS LKDRIAKYMV EEAERRRLLT PGQTIIEPTS
     GNTGISLAMI GRRKGYKVKV VVPENITVER RQLLELYGAE IIYSDARRGT NGAIEVAKKM
     ATLNRDWYMP YQYGNAENVR AHYETTGAEI LAALPHVDAF VAGLGTGGTL MGVGRRLKEV
     NPKTQVIAVE PHPGDLVQGL RSLDEGFIPP ILDLSLLDGK FLVDSRCAFA LTRDLTRKEG
     IFAGVSSGAV LHAAIRMAHK MNKGNIVCLL ADGGWKYVSL GVWAKELPDL GEDVYSHIWW
//
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