ID A0A0F5W4Z5_9ACTN Unreviewed; 461 AA.
AC A0A0F5W4Z5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Cystathionine beta-synthase {ECO:0000256|ARBA:ARBA00026192};
DE EC=4.2.1.22 {ECO:0000256|ARBA:ARBA00012041};
DE AltName: Full=Beta-thionase {ECO:0000256|ARBA:ARBA00030337};
DE AltName: Full=Serine sulfhydrase {ECO:0000256|ARBA:ARBA00031579};
GN ORFNames=TN53_07180 {ECO:0000313|EMBL:KKD08610.1};
OS Streptomyces sp. WM6386.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415558 {ECO:0000313|EMBL:KKD08610.1, ECO:0000313|Proteomes:UP000033641};
RN [1] {ECO:0000313|EMBL:KKD08610.1, ECO:0000313|Proteomes:UP000033641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6386 {ECO:0000313|EMBL:KKD08610.1,
RC ECO:0000313|Proteomes:UP000033641};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KKD08610.1}.
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DR EMBL; JXTE01000008; KKD08610.1; -; Genomic_DNA.
DR RefSeq; WP_046257540.1; NZ_JXTE01000008.1.
DR AlphaFoldDB; A0A0F5W4Z5; -.
DR PATRIC; fig|1415558.3.peg.8445; -.
DR OrthoDB; 9805733at2; -.
DR UniPathway; UPA00136; UER00201.
DR Proteomes; UP000033641; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004122; F:cystathionine beta-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProt.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:InterPro.
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 CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000033641}.
FT DOMAIN 336..400
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 461 AA; 49136 MW; D0AE28736451F3F0 CRC64;
MQFHDSMISL VGNTPLVRLN NVTKGIQATV LAKVEYFNPG GSVKDRIALR MIEAAEESGA
LKPGGTIVEP TSGNTGVGLA IVAQQKGYKC IFVCPDKVST DKINVLRAYG AEVVVCPTAV
DPEHPDSYYN VSDRLVRETP GAWKPDQYSN PNNPLSHYHS TGPELWEQTE GKITHFVAGV
GTGGTISGTG RYLKDASDGK VKVIGADPEG SVYSGGSGRP YLVEGVGEDF WPTAYDRTVA
DEIVAVSDKD SFQMTRRLAK EEGLLVGGSC GMAVVAALRV AEGLTEDDVV VVLLPDSGRG
YLSKIFNDEW LASYGFLEES EPTASVADVL RYKAGAIPSL VHMHPEETVG QAIEVLHEYG
VSQMPVVKPG AGHPDVMAAE VIGSIVERDL LDALFTQRAT LTDPLEKHMS SPLPQVGSGE
PIEDLMAVLG RADAAIVLVE GKPTGVVTRQ DLLAYMARAA Q
//
