ID A0A1H2CIZ9_9ACTN Unreviewed; 452 AA.
AC A0A1H2CIZ9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN04489716_5962 {ECO:0000313|EMBL:SDT70478.1};
OS Actinoplanes derwentensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=113562 {ECO:0000313|EMBL:SDT70478.1, ECO:0000313|Proteomes:UP000198688};
RN [1] {ECO:0000313|EMBL:SDT70478.1, ECO:0000313|Proteomes:UP000198688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43941 {ECO:0000313|EMBL:SDT70478.1,
RC ECO:0000313|Proteomes:UP000198688};
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; LT629758; SDT70478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2CIZ9; -.
DR STRING; 113562.SAMN04489716_5962; -.
DR OrthoDB; 9805733at2; -.
DR UniPathway; UPA00136; UER00201.
DR Proteomes; UP000198688; Chromosome i.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198688}.
FT DOMAIN 334..399
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 140..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 48173 MW; 91E263A2A7FE0902 CRC64;
MRYYDNVVEI IGNTPLVRLN SVTDGISATV LAKVEYMNPG GSVKDRIALR MVQDAEEAGL
LKPGGTIVEP TSGNTGVGLA LVAQLRGYKC VFVCPDKVSE DKQNVLRAYG AEVVVCPTAV
APEDPRSYYN VSDKLTRDIP GAWKPDQYSN PANPRSHYEQ TGPELWEQTG GKITHFVAGV
GTGGTITGVG RYLKEQGEVR VIGADPEGSV YSGGTGRPYL VEGVGEDFWP TAYDTSVTDE
VIEVSDSDSF EMTRRLAREE GLLVGGSCGM AVVAALEVAR KAGPDDVIVV LLPDGGRGYL
SKIFNDKWMA RYGFLRTQEG TPTVADALAG KAEGIPPLIH VHPTETVRDA IDYMREYGVS
QLPVLKAEPP VVTGEVAGSI SEKALLDALF TGQAHLHDTI ERHMGDPLPM IGGGEPVAEA
VGLLEKADAA MVLVDGKPAG VLTRQDLLAH LS
//
