ID B4S4R1_PROA2 Unreviewed; 457 AA.
AC B4S4R1;
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:ACF46957.1};
DE EC=2.5.1.47 {ECO:0000313|EMBL:ACF46957.1};
GN OrderedLocusNames=Paes_1945 {ECO:0000313|EMBL:ACF46957.1};
OS Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=290512 {ECO:0000313|EMBL:ACF46957.1, ECO:0000313|Proteomes:UP000002725};
RN [1] {ECO:0000313|EMBL:ACF46957.1, ECO:0000313|Proteomes:UP000002725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 271 / SK 413 {ECO:0000313|Proteomes:UP000002725};
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., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
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; CP001108; ACF46957.1; -; Genomic_DNA.
DR RefSeq; WP_012506490.1; NC_011059.1.
DR AlphaFoldDB; B4S4R1; -.
DR STRING; 290512.Paes_1945; -.
DR KEGG; paa:Paes_1945; -.
DR eggNOG; COG0031; Bacteria.
DR eggNOG; COG3620; Bacteria.
DR HOGENOM; CLU_021018_0_0_10; -.
DR Proteomes; UP000002725; 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; 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.
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:UP000002725};
KW Transferase {ECO:0000313|EMBL:ACF46957.1}.
FT DOMAIN 342..397
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 457 AA; 50306 MW; 8556A6495428174C CRC64;
MLQQNIFSMN AQVPMVAIKR LAAHIQPEIV ARLEYLNPSG THYWSVASVI IENAEKEGLI
SPGMTLVDWT YGSSGIALAM AAIAKGYKVL LVVPDKISRE KQQVLKAMGA EVVITPSDAL
PGAPRSCVNV AQNLVQNLKH AYFTNMYENP LSFSVHAETT GPMIWEQTGG EVTHLFVPVT
SGAMISGIGQ FLKSKRQNIR IIGVEPEGSI YRELLQHRKL SAPALFELEE IGGLWESKYW
DASVIDDIVQ VSDFDAFNCG RELLRSEAIF SGGSSGAAMF AALRAGAHLG RDARIVVMMS
DFGGYYLSKM YSDEWMKLKG FYRKAPSSRD EITAEDILGL KTRRDLIFAL PEHTLSEVFE
MMRQNDVSQL PIVSYGTAIG SISENKILSI LIENDDAMNS KVVGYMEQPF PVCPPHATIS
ELSEKLQENA SGVLISLSDG RLQLLTKSDL IEALTHK
//
