ID A0A0U3M7M3_9BURK Unreviewed; 489 AA.
AC A0A0U3M7M3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Cystathionine beta-synthase {ECO:0000313|EMBL:ALV04573.1};
GN ORFNames=DES44_4118 {ECO:0000313|EMBL:REG14105.1}, RD2015_67
GN {ECO:0000313|EMBL:ALV04573.1};
OS Roseateles depolymerans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=76731 {ECO:0000313|EMBL:ALV04573.1, ECO:0000313|Proteomes:UP000060699};
RN [1] {ECO:0000313|EMBL:ALV04573.1, ECO:0000313|Proteomes:UP000060699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42856 {ECO:0000313|EMBL:ALV04573.1,
RC ECO:0000313|Proteomes:UP000060699};
RA Kim K.M.;
RT "Complete genome of Roseateles depolymerans KCTC 42856.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:REG14105.1, ECO:0000313|Proteomes:UP000256283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11813 {ECO:0000313|EMBL:REG14105.1,
RC ECO:0000313|Proteomes:UP000256283};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|ARBA:ARBA00007103}.
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DR EMBL; CP013729; ALV04573.1; -; Genomic_DNA.
DR EMBL; QUMT01000004; REG14105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U3M7M3; -.
DR STRING; 76731.RD2015_67; -.
DR KEGG; rdp:RD2015_67; -.
DR PATRIC; fig|76731.3.peg.69; -.
DR OrthoDB; 9805733at2; -.
DR Proteomes; UP000060699; Chromosome.
DR Proteomes; UP000256283; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 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; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF191; 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 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000060699}.
FT DOMAIN 368..432
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 52352 MW; 9090D5F8807443EB CRC64;
MTTIDTAAPH RAANTSAPTG SAGSTAPVRA PFAGENARPA VLDLIGNTPL VPVRRLDTGP
CELFLKLESQ NPGGSIKDRI GLSMIEAAER DGLLPPGGTV VEATAGNTGL GLALVARAKG
YRVVLVVPDK MSAEKVLQLK ALGAEVHMTR SDVGKGHPDY YQDRAAKLVQ DIPGAWYADQ
FNNPANPLAH ETTTGPEIWQ QTGHRIDALV CGVGSGGTMT GLSRFFAKVR PGLDLVLADP
EGSVLKDYVE TGHYGEAGSW AVEGIGEDFI PPIADLSGVR HAYAVSDTDS FATARELYRA
EGILAGSSSG TLLAAALRYC RAQTTPKRVV TFVCDTGTRY LSKVYNDPWM FDQGLLQRAH
LGDLRDLISR RTEDGAVVSV SPEDTLATAF SRMRQADVSQ LPVLQQGRLV GLLDESDLLA
QMHMDARHFK DPVTSAMSHD VQTLPPGAPL SALIEQLRRG LVAVIADDQR FYGLVTRFDL
LNHLRKGLS
//
