ID H6MSH1_GORPV Unreviewed; 466 AA.
AC H6MSH1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=cystathionine beta-synthase {ECO:0000256|ARBA:ARBA00012041};
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 Name=cysB {ECO:0000313|EMBL:AFA72548.1};
GN OrderedLocusNames=GPOL_c14990 {ECO:0000313|EMBL:AFA72548.1};
OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA72548.1, ECO:0000313|Proteomes:UP000009154};
RN [1] {ECO:0000313|EMBL:AFA72548.1, ECO:0000313|Proteomes:UP000009154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA Liebl W., Daniel R., Steinbuchel A.;
RT "Involvement of two latex-clearing proteins during rubber degradation and
RT insights into the subsequent degradation pathway revealed by the genome
RT sequence of Gordonia polyisoprenivorans strain VH2.";
RL Appl. Environ. Microbiol. 78:2874-2887(2012).
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 -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|ARBA:ARBA00007103}.
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DR EMBL; CP003119; AFA72548.1; -; Genomic_DNA.
DR RefSeq; WP_014359406.1; NC_016906.1.
DR AlphaFoldDB; H6MSH1; -.
DR STRING; 1112204.GPOL_c14990; -.
DR KEGG; gpo:GPOL_c14990; -.
DR eggNOG; COG0031; Bacteria.
DR eggNOG; COG3620; Bacteria.
DR HOGENOM; CLU_021018_0_0_11; -.
DR OMA; WMADYGF; -.
DR Proteomes; UP000009154; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004122; F:cystathionine beta-synthase activity; IEA:UniProtKB-EC.
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; 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.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AFA72548.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000009154}.
FT DOMAIN 340..401
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 466 AA; 48805 MW; 7A1C180E2345AAFE CRC64;
MRIANHVVDL VGNTPLVKLN SVVTPGSGLV AAKVEYLNPG GSSKDRIALR MIEAAEKSGA
LKPGGTIVEP TSGNTGVGLA LVAQQRGYHC VFVCPDKVGE DKRNVLRAYG AEVVVCPTAV
APEHPDSYYN VSDRLVREID GAWKPNQYAN PAGPQSHYET TGPEIWADTD GTVTHFVAGV
GTGGTITGTG RYLKEVSGGA VKVVGVDPEG SVYSGGTGRP YLVEGVGEDF WPEAYDPSVP
DEIIAVSDAD SFDMTRRLAR EEGLLVGGSC GMAVVAALRV AEREGPDAVV VVLLPDGGRG
YMAKIFNDEW MSSYGFLRTP LDAKATEPLV GDVLRGKTGA LPDLVHTHPS ETLRDAIEIL
REYGVSQMPV VGAEPPVMAG EVAGAVTERD LLSAVFEGRA NLADPVSAHM GEPFPLIGSG
EPVSAATKAL SDTDALMVVE DGKPIGVITR HDLLAFVSTH PTITAG
//