ID B4SFD6_PELPB Unreviewed; 457 AA.
AC B4SFD6;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Cysteine synthase {ECO:0000313|EMBL:ACF44715.1};
DE EC=2.5.1.47 {ECO:0000313|EMBL:ACF44715.1};
GN OrderedLocusNames=Ppha_2553 {ECO:0000313|EMBL:ACF44715.1};
OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=324925 {ECO:0000313|EMBL:ACF44715.1, ECO:0000313|Proteomes:UP000002724};
RN [1] {ECO:0000313|EMBL:ACF44715.1, ECO:0000313|Proteomes:UP000002724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5477 / BU-1 {ECO:0000313|Proteomes:UP000002724};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; CP001110; ACF44715.1; -; Genomic_DNA.
DR RefSeq; WP_012509188.1; NC_011060.1.
DR AlphaFoldDB; B4SFD6; -.
DR STRING; 324925.Ppha_2553; -.
DR KEGG; pph:Ppha_2553; -.
DR eggNOG; COG0031; Bacteria.
DR eggNOG; COG3620; Bacteria.
DR HOGENOM; CLU_021018_0_0_10; -.
DR OrthoDB; 9808024at2; -.
DR Proteomes; UP000002724; Chromosome.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR CDD; cd01561; CBS_like; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
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; 1.
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.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000002724};
KW Transferase {ECO:0000313|EMBL:ACF44715.1}.
FT DOMAIN 342..397
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 457 AA; 50234 MW; ECF90D14B5F1BFEC CRC64;
MSNHDIFGLA TETPMVSVKQ MARQISPKVM AKLEYMNPAC SHYYRVASAI VRDAEERKLI
HPGMTLVDWT FGNSGIALAM AGVSRGYKLL LAAPDKISQE KQHMLRALGA ELVITPSDAL
PGEERSCMNV AESLERSISN SFFTGMYKNP LSLKVHREAT GSEIYRQTEG RVTHVFVPMV
SGAMVFGIGA FLKAKNPKIQ IIGVESQGSI YASLFRDGMP GDPALSELEE LGSRQPSAFW
DPSVLDDVVQ VSDYDAFNCA RELLRMEAVF GGGASGAAMA AALRAGASYG PDDCVVAVMN
DFGGYYLSKM YRDEWMRKHG FYRKVKSALE QITAEDILHL KVRRDLIFAY PENTLAEVFE
MMKQSDVSQL PIVSYNAPIG SISENKILSI LIENDDAMNA KVVGFMERPF PVCRLDATIS
ELSDKLQQSA SGVLISLSDG RLQLLTKSDL IDALTHK
//
