ID G2NEC1_STREK Unreviewed; 467 AA.
AC G2NEC1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=SACTE_2542 {ECO:0000313|EMBL:AEN10430.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN10430.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN10430.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN10430.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(2014).
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 -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|ARBA:ARBA00007103}.
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DR EMBL; CP002993; AEN10430.1; -; Genomic_DNA.
DR RefSeq; WP_014046414.1; NC_015953.1.
DR AlphaFoldDB; G2NEC1; -.
DR STRING; 862751.SACTE_2542; -.
DR KEGG; ssx:SACTE_2542; -.
DR PATRIC; fig|862751.12.peg.2647; -.
DR eggNOG; COG0031; Bacteria.
DR eggNOG; COG3620; Bacteria.
DR HOGENOM; CLU_021018_0_0_11; -.
DR OrthoDB; 9805733at2; -.
DR UniPathway; UPA00136; UER00201.
DR Proteomes; UP000001397; Chromosome.
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 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; 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; 2.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 3: Inferred from homology;
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:UP000001397}.
FT DOMAIN 336..400
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 409..466
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 141..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 49736 MW; D35FE994D48D0BB8 CRC64;
MQFHDSMISL VGNTPLVRLR NVSAGIQATV LAKVEYFNPG GSVKDRIALR MIEAAEQSGE
LKPGGTIVEP TSGNTGVGLA IVAQQKGYRC IFVCPDKVST DKINVLRAYG AEVVVCPTAV
DPEHPDSYYN VSDRLVRETP GAWKPDQYSN PNNPRSHYET TGPELWEQTE GKITHFVAGV
GTGGTITGTG RYLKEVSGDK VRIVGADPEG SVYSGGSGRP YLVEGVGEDF WPSAYDRTVT
DEIVAVSDKD SFQMTRRLAK EEGLLVGGSC GMAVVGALEV AKRLGPDDVV VVLLPDSGRG
YLSKIFNDEW MADYGFLEDT GTSARVGAVL DFKEGPLPSL VHMHPEETVG EAIDVLREYG
VSQMPIVKPG AGHPDVMAAE VIGSVVERQL LDALFTQRAS LSDPLEKHMS APLPQVGSGE
PVEDLMAVLS GTEGADAAIV LVEGKPKGVV SRQDLLAFLA KGAAPKQ
//
