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Database: UniProt
Entry: A0A1S1Q8J9_9ACTN
LinkDB: A0A1S1Q8J9_9ACTN
Original site: A0A1S1Q8J9_9ACTN 
ID   A0A1S1Q8J9_9ACTN        Unreviewed;       315 AA.
AC   A0A1S1Q8J9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Cysteine synthase B {ECO:0000313|EMBL:OHV29937.1};
GN   Name=cysM {ECO:0000313|EMBL:OHV29937.1};
GN   ORFNames=BCD49_35120 {ECO:0000313|EMBL:OHV29937.1};
OS   Pseudofrankia sp. EUN1h.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Pseudofrankia.
OX   NCBI_TaxID=1834515 {ECO:0000313|EMBL:OHV29937.1, ECO:0000313|Proteomes:UP000179465};
RN   [1] {ECO:0000313|Proteomes:UP000179465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EUN1h {ECO:0000313|Proteomes:UP000179465};
RA   Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA   Nouioui I., Abebe-Akele F., Thomas K., Gtari M., Tisa L.S.;
RT   "Sequence Frankia sp. strain EUN1h.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR605856-50};
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:OHV29937.1}.
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DR   EMBL; MBLN01000095; OHV29937.1; -; Genomic_DNA.
DR   RefSeq; WP_071042405.1; NZ_MBLN01000095.1.
DR   Proteomes; UP000179465; Unassembled WGS sequence.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; IPR000634; Ser/Thr_deHydtase_PyrdxlP-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:SF162; CYSTEINE SYNTHASE B; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..287
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         73
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         176..180
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         257
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         43
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   315 AA;  33962 MW;  E4E644E2984594EC CRC64;
     MRYDSLVGSV GRTPLVGLPR LSPSADVRLW AKLEQDNPTG SIKDRAALWM VQDAEKRGVL
     SPGAMVLEPT SGNTGISLAM VCRQRGYRLT CVMPENTSIE RRQLLAMWGA EIIFSPAAGG
     SNEAVAVAKR LSAQHPDWVM LYQYGNPANA QAHYETTGPE ILEDLPSITH FVAGLGTTGT
     LMGTGRYLRE RVPGITIVAA EPRYGELVYG LRNIDEGFVP ELYDPAVLTS RYSVGPKEAL
     RRTXELVAEE GIFAGISTGA ILHAALGQAD RAVKEGRRAD IAFIVCDGGW KYLSTGAYAG
     TLEEAEAALE GQLWA
//
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