ID B0X072_CULQU Unreviewed; 539 AA.
AC B0X072;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Cystathionine beta-synthase {ECO:0000256|ARBA:ARBA00026192, ECO:0000256|RuleBase:RU361204};
DE EC=4.2.1.22 {ECO:0000256|ARBA:ARBA00012041, ECO:0000256|RuleBase:RU361204};
GN Name=6045737 {ECO:0000313|EnsemblMetazoa:CPIJ012753-PA};
GN ORFNames=CpipJ_CPIJ012753 {ECO:0000313|EMBL:EDS37947.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS37947.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS37947.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ012753-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ012753-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homocysteine + L-serine = H2O + L,L-cystathionine;
CC Xref=Rhea:RHEA:10112, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:58161, ChEBI:CHEBI:58199; EC=4.2.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00001175,
CC ECO:0000256|RuleBase:RU361204};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU361204};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-homocysteine and L-serine: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005003}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|ARBA:ARBA00007103,
CC ECO:0000256|RuleBase:RU361204}.
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DR EMBL; DS232229; EDS37947.1; -; Genomic_DNA.
DR RefSeq; XP_001863044.1; XM_001863009.1.
DR AlphaFoldDB; B0X072; -.
DR STRING; 7176.B0X072; -.
DR EnsemblMetazoa; CPIJ012753-RA; CPIJ012753-PA; CPIJ012753.
DR GeneID; 6045737; -.
DR KEGG; cqu:CpipJ_CPIJ012753; -.
DR VEuPathDB; VectorBase:CPIJ012753; -.
DR VEuPathDB; VectorBase:CQUJHB004007; -.
DR eggNOG; KOG1252; Eukaryota.
DR HOGENOM; CLU_021018_0_0_1; -.
DR InParanoid; B0X072; -.
DR OMA; KFADDEW; -.
DR OrthoDB; 5487987at2759; -.
DR UniPathway; UPA00136; UER00201.
DR Proteomes; UP000002320; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004122; F:cystathionine beta-synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:UniProtKB-UniRule.
DR CDD; cd01561; CBS_like; 1.
DR CDD; cd04608; CBS_pair_CBS; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR046353; CBS_C.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR005857; Cysta_beta_synth.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01137; cysta_beta; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF194; CYSTATHIONINE BETA-SYNTHASE; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00291; PALP; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU361204};
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192,
KW ECO:0000256|RuleBase:RU361204};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361204};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU361204};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320}.
FT DOMAIN 401..460
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 539 AA; 58344 MW; 218A55170C70C9A9 CRC64;
MSDHRTCPMA NGHNGTSSTN GGVDSREQFL AGFKRPDLAS RCTWAVGTEE ASPHQHRPLV
PRPKVLQTIL QAVGNTPLVK LNSIPKAANL KCNLYAKCEF MSPGGSVKDR IGLRMIEEAE
KKGLLKPGYT IIEPTSGNTG IGLAMGAAVK GYRCLIVMPE KMSNEKVDTL KALGAEVIRT
PTEAAFDSPE GLIAVAQRLE KEIPNSIVLN QYTNAGNPLA HYDGTGAEIV DQLEGQVDMV
VVGAGTGGTV AGIGRKIKET NPDCVIVGAD PEGSILALPD KLNESNVSFY EVEGVGYDFI
PTVLDRSVVD RWIKFNDKDA LPMARRLIAE EGFLCGGSSG GNVAVALEAA KELKEGQNCV
VILPDNIRNY LTKFVSDNWM EARNFKPSVN VHKHKWWNNS LTTLDMTPPP TVGVDVCLQE
VINIMQTAHV DHLPVLDGTT VKGMVSLPNL TSKLLNRLAK PSDPVSRAIF KQFVRVDQND
NVGHVSRILE KDAFVLVVKN EKTSDSQLKE TVVGVLTQRD LLFYISNAQN VINGDGNSA
//
