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Database: UniProt
Entry: H6MSH1_GORPV
LinkDB: H6MSH1_GORPV
Original site: H6MSH1_GORPV 
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
//
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