ID Q2RWA4_RHORT Unreviewed; 454 AA.
AC Q2RWA4;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Cystathionine beta-synthase {ECO:0000313|EMBL:ABC21591.1};
DE EC=4.2.1.22 {ECO:0000313|EMBL:ABC21591.1};
GN OrderedLocusNames=Rru_A0787 {ECO:0000313|EMBL:ABC21591.1};
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC21591.1, ECO:0000313|Proteomes:UP000001929};
RN [1] {ECO:0000313|EMBL:ABC21591.1, ECO:0000313|Proteomes:UP000001929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1
RC {ECO:0000313|Proteomes:UP000001929};
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
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; CP000230; ABC21591.1; -; Genomic_DNA.
DR RefSeq; WP_011388545.1; NC_007643.1.
DR RefSeq; YP_425878.1; NC_007643.1.
DR AlphaFoldDB; Q2RWA4; -.
DR STRING; 269796.Rru_A0787; -.
DR EnsemblBacteria; ABC21591; ABC21591; Rru_A0787.
DR KEGG; rru:Rru_A0787; -.
DR PATRIC; fig|269796.9.peg.840; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_021018_0_0_5; -.
DR PhylomeDB; Q2RWA4; -.
DR Proteomes; UP000001929; Chromosome.
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 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 Lyase {ECO:0000313|EMBL:ABC21591.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001929}.
FT DOMAIN 334..396
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 454 AA; 48691 MW; E2457FF5692DD33C CRC64;
MTAPVDLLAQ IGHTPIVRLD HLDTGPCSLF VKLESQNPSG SIKDRIAVSM IDAAERDGRL
KPKGRIVEAT AGNTGLALAL VAARRGYHLT LVIPDKMSRE KIAHVRAMGA EVVLTRSDIG
KGHPAYYQDL AQRIADETGA FFTDQFNNPD NPIAHETGTG PEIWEQMDGR VDAVVAGVGS
GGTLTGLSRF FARVSPQTDI VLADPKGSIL ADYVTSGRIG AAGSWLVEGI GEDFVPPVSD
LSRVTHAYTI PDGESFATAR GVLRQEGLLI GSSSGTLLAA ALRYCREQTS PKRVVSFVCD
SGNKYLSKMY NDFWMADQGL SNRPRFGDLR DLIARRQDEG AVVSVAPGDT LAIAYQRMKL
YDVSQLPVLD GTRCVGLIDE SDVLLSLRER GGLFDVAVSA AMSTDLETVG PDADADHLVG
LFDRGRVAIV VDDSGFLGLI TRIDFLNHLR GKAA
//