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Database: UniProt
Entry: A0A1H5C1Q6_9PSEU
LinkDB: A0A1H5C1Q6_9PSEU
Original site: A0A1H5C1Q6_9PSEU 
ID   A0A1H5C1Q6_9PSEU        Unreviewed;       469 AA.
AC   A0A1H5C1Q6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=SAMN04489727_8545 {ECO:0000313|EMBL:SED60391.1};
OS   Amycolatopsis tolypomycina.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=208445 {ECO:0000313|EMBL:SED60391.1, ECO:0000313|Proteomes:UP000199622};
RN   [1] {ECO:0000313|EMBL:SED60391.1, ECO:0000313|Proteomes:UP000199622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44544 {ECO:0000313|EMBL:SED60391.1,
RC   ECO:0000313|Proteomes:UP000199622};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNSO01000004; SED60391.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5C1Q6; -.
DR   STRING; 208445.SAMN04489727_8545; -.
DR   UniPathway; UPA00136; UER00201.
DR   Proteomes; UP000199622; 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}; Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          349..411
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   469 AA;  49283 MW;  E2EA52FD0A44E8C2 CRC64;
     MDNATGGPFR LAVVEYAEHI ADLVGNTPLV RLNSLTKGLK PLVLAKVEYL NPGGSVKDRI
     ALRMIEAAEA AGELRPGGTI VEPTSGNTGV GLAMVAQRKG YQCVFVCPDK VSEDKRNVLK
     AYGARVVVCP TAVPPEHPDS YYNVSDRLVR EIEGAWKPNQ YANPQNPESH YHSTGPELWT
     QTGGKITHFV AGVGTGGTIS GTGRYLKEVS DGAVQVVGAD PEGSVYSGGS GRPYLVEGVG
     EDFWPDTYDR GIADEIIPVS DADSFQVTRR LALEEGLLVG GSCGMAVAAA LKLAERLTED
     DVVVVLLPDG GRGYLTKVFN DTWMSSYGFL PPDSSGATVA DVLTKKSGSL PDLVHSHPNE
     TVAEAIAILS EFGVSQMPVV SAEPPVMAAE VVGAVNERDL LDALFTGKAQ LADRLEQHMS
     PPLPTIGGGE QVSAAMTALE GADGALVLVD GKPAGVVTRH DLLGFLAGR
//
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