ID W7IDJ6_9PSEU Unreviewed; 316 AA.
AC W7IDJ6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cysteine synthase B {ECO:0000313|EMBL:EWC58588.1};
DE EC=2.5.1.47 {ECO:0000313|EMBL:EWC58588.1};
GN ORFNames=UO65_6134 {ECO:0000313|EMBL:EWC58588.1};
OS Actinokineospora spheciospongiae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC58588.1, ECO:0000313|Proteomes:UP000019277};
RN [1] {ECO:0000313|EMBL:EWC58588.1, ECO:0000313|Proteomes:UP000019277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EG49 {ECO:0000313|EMBL:EWC58588.1,
RC ECO:0000313|Proteomes:UP000019277};
RX PubMed=24604655;
RA Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA Hentschel U.;
RT "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT Bacterium Actinokineospora sp. Strain EG49.";
RL Genome Announc. 2:e00160-14(2014).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR605856-50};
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|ARBA:ARBA00007103}.
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:EWC58588.1}.
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DR EMBL; AYXG01000237; EWC58588.1; -; Genomic_DNA.
DR RefSeq; WP_035289465.1; NZ_AYXG01000237.1.
DR AlphaFoldDB; W7IDJ6; -.
DR STRING; 909613.UO65_6134; -.
DR PATRIC; fig|909613.9.peg.6133; -.
DR eggNOG; COG0031; Bacteria.
DR OrthoDB; 9805733at2; -.
DR Proteomes; UP000019277; Unassembled WGS sequence.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
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; IPR005856; Cys_synth.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01136; cysKM; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF255; O-PHOSPHOSERINE SULFHYDRYLASE; 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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR605856-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000019277};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EWC58588.1}.
FT DOMAIN 9..288
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT BINDING 74
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 177..181
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 258
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT MOD_RES 44
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 316 AA; 34003 MW; 9541FE5038647B7D CRC64;
MARYDSLLDA LGDTPLVGLP RLSPSADVRL WAKLEDRNPT GSIKDRPALA MITAAERDGV
LLPGNTILEP TSGNTGISLA MAAKLKGYGL VCVMPENTSE ERRTLLQAYG ARIVFSPAAG
GSNEAVRRAK ELAKEHPDWV MLYQYGNPDN AGAHYRGTGP EILRDLPSIT HFVAGLGTTG
TLVGVGRYLR EQKPDVEIVA AEPRYGELVY GLRNLDEGFV PELYDPEVLT GRYSVGSYDA
LRRTRQLLET EGIFAGISTG AILHAALSVA EKVANRGGEA DIVFIVCDGG WKYLSTGAYS
GSLDEAAERL DGHLWA
//