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Database: UniProt
Entry: D8TK58_VOLCA
LinkDB: D8TK58_VOLCA
Original site: D8TK58_VOLCA 
ID   D8TK58_VOLCA            Unreviewed;       388 AA.
AC   D8TK58;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985};
DE            EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985};
GN   ORFNames=VOLCADRAFT_79370 {ECO:0000313|EMBL:EFJ52191.1};
OS   Volvox carteri f. nagariensis.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX   NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN   [1] {ECO:0000313|EMBL:EFJ52191.1, ECO:0000313|Proteomes:UP000001058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX   PubMed=20616280; DOI=10.1126/science.1188800;
RA   Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA   Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA   Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA   Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA   Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT   "Genomic analysis of organismal complexity in the multicellular green alga
RT   Volvox carteri.";
RL   Science 329:223-226(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC         Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC         Evidence={ECO:0000256|RuleBase:RU003985};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR605856-50, ECO:0000256|RuleBase:RU003985};
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000256|ARBA:ARBA00007103,
CC       ECO:0000256|RuleBase:RU003985}.
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DR   EMBL; GL378325; EFJ52191.1; -; Genomic_DNA.
DR   RefSeq; XP_002946965.1; XM_002946919.1.
DR   AlphaFoldDB; D8TK58; -.
DR   STRING; 3068.D8TK58; -.
DR   GeneID; 9618190; -.
DR   KEGG; vcn:VOLCADRAFT_79370; -.
DR   eggNOG; KOG1252; Eukaryota.
DR   InParanoid; D8TK58; -.
DR   OrthoDB; 313426at2759; -.
DR   Proteomes; UP000001058; Unassembled WGS sequence.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR   CDD; cd01561; CBS_like; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR005856; Cys_synth.
DR   InterPro; IPR005859; CysK.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01139; cysK; 1.
DR   NCBIfam; TIGR01136; cysKM; 1.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF241; CYSTEINE SYNTHASE, MITOCHONDRIAL; 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|RuleBase:RU003985};
KW   Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192,
KW   ECO:0000256|RuleBase:RU003985};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR605856-50,
KW   ECO:0000256|RuleBase:RU003985};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001058};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT   DOMAIN          60..347
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         128
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         232..236
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         320
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         97
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   388 AA;  40945 MW;  8550B05ED14E03CF CRC64;
     MQAVHTSRQA LRPFGKAGAR QHARRPLSLR LQASSGVVES TLAAAPADAP SKPKKICSDI
     TEVIGNTPMV YLNRVTKGCV ARVAAKLEIM QPCSSVKDRI GRNMIDDAEK RGAIKPGVTT
     LVEPTSGNTG IGLAFVAAAR GYKLILTMPA SMSLERRVLL RAFGAELVLT DPAKGMRGAV
     EKCNEIAAKT PNSYILQQFE NPANPEVHRL TTGPEIWRDT VGQVDILVAG VGTGGTVTGT
     GEYLKSVKQG LQVVAVEPAE SPVLSGGKPG PHRIQGIGAG FVPAILNTAV YDEVLKVQSD
     DAVAMAARLA TDEGLFCGIS SGAAVAAAIK VASRPENAGK LVVVVLPSFG ERYLSSVLFN
     QLRLECEALK QDERAKISDI AGREFFVP
//
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