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Database: UniProt
Entry: X8AEB1_MYCXE
LinkDB: X8AEB1_MYCXE
Original site: X8AEB1_MYCXE 
ID   X8AEB1_MYCXE            Unreviewed;       413 AA.
AC   X8AEB1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Putative cystathionine beta-synthase {ECO:0000313|EMBL:EUA29849.1};
GN   ORFNames=I553_4102 {ECO:0000313|EMBL:EUA29849.1};
OS   Mycobacterium xenopi 4042.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1299334 {ECO:0000313|EMBL:EUA29849.1};
RN   [1] {ECO:0000313|EMBL:EUA29849.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4042 {ECO:0000313|EMBL:EUA29849.1};
RA   Brown-Elliot B., Wallace R., Lenaerts A., Ordway D., DeGroote M.A.,
RA   Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA   Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL   Submitted (JAN-2014) 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:EUA29849.1}.
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DR   EMBL; JAOB01000060; EUA29849.1; -; Genomic_DNA.
DR   AlphaFoldDB; X8AEB1; -.
DR   PATRIC; fig|1299334.3.peg.5794; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProt.
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; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF194; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF00291; PALP; 2.
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.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          289..351
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   413 AA;  43430 MW;  7845D0D812A5EC6E CRC64;
     MIDAAEASGQ LKPGGTIVEP TSGNTGVALA MVAQQRGYKC VFVCPDKVSE DKQNVLRAYG
     PKSWCARRRC HPTTRTATTA CPTGWSPRST APGSRTSTRI PTGRQAITRR LDRKSGPTPT
     AGSHTSWPGS APADDYGRGP LPQGGVRGAV RVIGADPEGS VYSGGTGRPY LVEGVGEDFW
     PAAYDPTVPD EVIAVSDADS FEMTRRLARE EAMLVGGSCG MAVVAALKVA EDAGPDALIV
     VLLPDGGRGY MSKIFNDAWM SSYGFLRSRL DGSMQQPTVG DVLRGKSGAL PDLVHTHPSE
     TVRDAIGILR EYGVSQMPVV GAEPPVMAGE VVGSVSEREL LSAVFEGRAK LADAVSLHMS
     PPLPMIGAGE LITAAAKALR DADALMVVEE GKPVGVITRH DLLGFLSEGP RRR
//
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