ID A0A0Q6WPX5_9BURK Unreviewed; 458 AA.
AC A0A0Q6WPX5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Cystathionine beta-synthase {ECO:0000313|EMBL:KQV87872.1};
GN ORFNames=ASD15_27880 {ECO:0000313|EMBL:KQV87872.1};
OS Massilia sp. Root351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV87872.1, ECO:0000313|Proteomes:UP000051876};
RN [1] {ECO:0000313|EMBL:KQV87872.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV87872.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV87872.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV87872.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQV87872.1}.
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DR EMBL; LMDJ01000005; KQV87872.1; -; Genomic_DNA.
DR RefSeq; WP_057154711.1; NZ_LMDJ01000005.1.
DR AlphaFoldDB; A0A0Q6WPX5; -.
DR OrthoDB; 9805733at2; -.
DR Proteomes; UP000051876; 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:UP000051876}.
FT DOMAIN 341..397
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 458 AA; 49464 MW; 2D7E4AA8731F818D CRC64;
MNKPHEAALF GLIGNTPLIE VTRLDTGPCR LFLKLESQNP GGSIKDRIGL SIIEAAERDG
RLKPGGVIIE ATAGNTGLGL ALVGRIKGYR VVLVVPDKMS TEKVLHLKAL GAEVHMTRSD
VGKGHPEYYQ DYAARLAREL PGAFYADQFN NPANPLAHET TTAPEIWEQM AHEVDAIVVG
VGSSGTLTGL SNFFRKVQPQ LEFVLADPKG SILAEYIASG KVSDTSGSWA VEGIGEDFIP
SIADMRSVRK AYTISDQESF DSARALLSAE GVLGGSSTGT LLAAALKYCR EQTAPKRVVT
FVADTGTRYL SKMYNHGWLV DQGMVQRAQT GDLRDLIGRR YDEGDVVSVA PSDTLLVAFN
RMRAADLAQL PVLEQGKLVG IIDESDLLLK VDNHAEQFSS LVGATMTARL ETLHPSASVQ
ALRSTLDRGL TAVVADSSKF YGLITRFDLL NHLRRTLS
//
