ID A0A150H0L3_GONPE Unreviewed; 1219 AA.
AC A0A150H0L3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985};
DE EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985};
GN ORFNames=GPECTOR_2g1256 {ECO:0000313|EMBL:KXZ55706.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ55706.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
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=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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}.
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:KXZ55706.1}.
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DR EMBL; LSYV01000003; KXZ55706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150H0L3; -.
DR STRING; 33097.A0A150H0L3; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR005856; Cys_synth.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR005859; CysK.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
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; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF00291; PALP; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
DR PROSITE; PS51384; FAD_FR; 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}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR605856-50,
KW ECO:0000256|RuleBase:RU003985};
KW Reference proteome {ECO:0000313|Proteomes:UP000075714};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT DOMAIN 437..715
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 104..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 973
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 1077..1081
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 1165
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT MOD_RES 942
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 1219 AA; 126195 MW; F96595B7CC591844 CRC64;
MAAAEESAAN AAAAEEAAAK AAAEEAAAMA VAEEAAAKAA AEEEAAAKAA AKEAAAMAAA
EEAAAKAAAE EAAVKAAAEE AAAMAAAEEA AVKAAAEEAA AMAAAEEAAA KAAAEEAAAK
AAEEEATAKA AAEEAAAKAA AEEAAAKAAA EEAAAKAAAE EAAAKAAAEE AAAKAAAEEA
AAKAAAEEAA AKAEAAKAAA REATTKAAEE GAAKAAEGDA AAKAAAEKVA ADEAAAKAAE
AEATEMAASE DAAAKAAAEE AAAKAAAKTA AEEAAAKAAA EETAQSNEDE PDPLLTPSDS
ISRSVSPSVV GHGSPAEKVR RAAEVVKKAH DAAEAARRRR SIEKPPSRLQ AKPINVNFPK
REEQVVKRKD EKGYGMLMGL APVGVDTKTA PALLPPRIKI STEKDEGRAK AVREREAARP
TREERHKLDP AGNYSAAQPF WAHISDASYE TAFWSDRKVL HLELSIRGSN MAYEPGDAIG
VLPVNHPDLV ANLCKRLKQN PDRVLHIHAA PAGVAGAGAD GASDVASVDG RSASPAQAAS
EGRVASHLPS PASLGYLLSH CVDLTGVTRK SVLRLLAEHT HDAAEKRTLL YLSARGGKEA
YAHEITEHQP SLLDLLVRFP SCNPPLDALL DGLPPLAPRM YSVSSSRRDP ARGPNRLSVT
LSVVRFKTRY GTRLGVATTW LERLAAPFAL EGAEPPAEPI WVPIYLRRAA DFKPPTDLAT
PLIMVGPGTG VAPFRGFLQE RRAVIAERKP APESVGEAVL FFGCRREDED YLYQADLEGF
KADGTLSALH VAFSRAKADR VYVQDLLKEQ GEKVWALLQA GAHVYVCGDG ASMAKDVHAA
LANIAVQHGS LSEQDATAYL QLQRARSAAL NSARSAPVRA PRAVVKPQAI AAADKGLEMN
IATDVTQLIG KTPMVYLSKV TKGCAAKVAA KLEIMEPCCS VKDRIGYSMI TEAEKEGKII
PGKTTLVEPT SGNTGIGLAF IAAARGYKLI LTMPASMSLE RRILLRAFGA ELVLTDPAKG
MKGAVAKAEE ILASTPDAFM LQQFQNPANP KVHYETTGPE IWDASDGAVD ILISGVGTGG
TITGTGRYLR EKKPSVQLVA VEPAESPVLS GGKPGPHKIQ GIGAGFVPAV LDTAIISEVV
QVSSDDAIEM ARRLALEEGL MVGISSGAAV AAAIKVANRP ENKDKLVVVV LPSFGERYLS
SVLFQQLRDE ASKMTFEAA
//