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Database: UniProt
Entry: A0A372J3V2_9ACTN
LinkDB: A0A372J3V2_9ACTN
Original site: A0A372J3V2_9ACTN 
ID   A0A372J3V2_9ACTN        Unreviewed;       468 AA.
AC   A0A372J3V2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=D0Z06_09555 {ECO:0000313|EMBL:RFU21857.1};
OS   Geodermatophilus sp. LHW52908.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=2303986 {ECO:0000313|EMBL:RFU21857.1, ECO:0000313|Proteomes:UP000262362};
RN   [1] {ECO:0000313|EMBL:RFU21857.1, ECO:0000313|Proteomes:UP000262362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW52908 {ECO:0000313|EMBL:RFU21857.1,
RC   ECO:0000313|Proteomes:UP000262362};
RA   Li L., Lin H.W.;
RT   "Geodermatophilus marinus sp. nov., isolated from marine sponge Leucetta
RT   chagosensis.";
RL   Submitted (AUG-2018) 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   -!- 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:RFU21857.1}.
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DR   EMBL; QVQH01000006; RFU21857.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372J3V2; -.
DR   OrthoDB; 9805733at2; -.
DR   UniPathway; UPA00136; UER00201.
DR   Proteomes; UP000262362; 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   Gene3D; 3.40.50.1100; -; 2.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
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   4: Predicted;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW   ProRule:PRU00703};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:RFU21857.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000262362}.
FT   DOMAIN          338..399
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   REGION          142..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  48901 MW;  95151F415EA0B49A CRC64;
     MQYAESVVDL VGNTPLVRLT SVTRDLGPAA PLVLAKVEYL NPGGSVKDRI AVRMVDAAEA
     SGALRPGGTI VEPTSGNTGI GLALVAQQRG YRCVFVCPDK VGQEKVNVLR AYGAEVVVCP
     TAVDPADPRS YYSVSDRLAR ETPGGWKPDQ YSNPANPQSH YETTGPEIWA QTDGRVTHFV
     TGMGTGGTIS GVGRYLKEAS DGRVRVIGAD PEGSVYSGGT GRPYLVEGVG EDFWPSTYDR
     GVADEVIAVS DGDSFAMTRR LAREEGLLVG GSCGMAVVAA LRAAERLTAD DVLVVLLPDG
     GRGYLGKIFN DEWMADYGFL EETGGETVGE LLTGKGGTTP ELVHTHPNET VREAIDILRE
     YGVSQLPVVR AEPPVTAGEV VGSVGEKVLL DALFAGRANL SDRIERHMSP PLPIIGSGEP
     VSAAVAALGS ADALLVHEDG KPAGVVTRQD VLGHLVGHPA GLGPTVGA
//
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