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Database: UniProt
Entry: A0A1I2FT36_9ACTN
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Original site: A0A1I2FT36_9ACTN 
ID   A0A1I2FT36_9ACTN        Unreviewed;       462 AA.
AC   A0A1I2FT36;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-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=SAMN05216251_10859 {ECO:0000313|EMBL:SFF08562.1};
OS   Actinacidiphila alni.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=380248 {ECO:0000313|EMBL:SFF08562.1, ECO:0000313|Proteomes:UP000199323};
RN   [1] {ECO:0000313|EMBL:SFF08562.1, ECO:0000313|Proteomes:UP000199323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFF08562.1,
RC   ECO:0000313|Proteomes:UP000199323};
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; L-cysteine biosynthesis; L-cysteine
CC       from L-homocysteine and L-serine: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005003}.
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DR   EMBL; FONG01000008; SFF08562.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2FT36; -.
DR   STRING; 380248.SAMN05216251_10859; -.
DR   OrthoDB; 9805733at2; -.
DR   UniPathway; UPA00136; UER00201.
DR   Proteomes; UP000199323; 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; 1.
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:UP000199323}.
FT   DOMAIN          336..400
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   REGION          141..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   462 AA;  49015 MW;  12DA2F18065899A2 CRC64;
     MQFHDSMISL VGNTPLVRLN SVTEGIQATV LAKVEYFNPG GSVKDRIALR MIEAAERSGD
     LKPGGTIVEP TSGNTGVGLA IVAQQKGYHC VFVCPDKVST DKINVMRAYG AEVVVCPTAV
     DPSHPDSYYN VSDRLVRETP NAWKPDQYSN PDNPASHYHS TGPELWEQTE GRITHFVAGV
     GTGGTISGTG RYLKDASEGR VQVVGADPEG SVYSGGSGRP YLVEGVGEDF WPDAYDRDVA
     DEIVAVSDKD SFQMTRRLAK EEGLLVGGSC GMAVVAALEV ARRLGPDDVV VVLLPDSGRG
     YLSKIFSDEW MSSHGFLDEG DGQARVADVL GHKDGGLPQL VHMHPDETVG EAIDVLREYG
     VSQMPVVKPG AGHPDVMAAE VIGSVVERDL LHALFTKRAT LEDPLDKHLS APLPQVGSGE
     PVAVLMTVLE SADAAIVLVD GKPTGVVSRQ DLLAFLAGHG GA
//
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