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Database: UniProt
Entry: C3MCJ0_SINFN
LinkDB: C3MCJ0_SINFN
Original site: C3MCJ0_SINFN 
ID   C3MCJ0_SINFN            Unreviewed;       346 AA.
AC   C3MCJ0;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Cysteine synthase protein {ECO:0000313|EMBL:ACP25269.1};
DE            EC=2.5.1.47 {ECO:0000313|EMBL:ACP25269.1};
GN   Name=cysK2 {ECO:0000313|EMBL:ACP25269.1};
GN   OrderedLocusNames=NGR_c14980 {ECO:0000313|EMBL:ACP25269.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP25269.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP25269.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; CP001389; ACP25269.1; -; Genomic_DNA.
DR   RefSeq; WP_012708041.1; NC_012587.1.
DR   RefSeq; YP_002826022.1; NC_012587.1.
DR   AlphaFoldDB; C3MCJ0; -.
DR   STRING; 394.NGR_c14980; -.
DR   KEGG; rhi:NGR_c14980; -.
DR   PATRIC; fig|394.7.peg.4311; -.
DR   eggNOG; COG0031; Bacteria.
DR   HOGENOM; CLU_021018_1_0_5; -.
DR   OrthoDB; 9805733at2; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   CDD; cd01561; CBS_like; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
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:SF211; PALP DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Transferase {ECO:0000313|EMBL:ACP25269.1}.
FT   DOMAIN          8..306
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   346 AA;  36387 MW;  E325BB538FE75A29 CRC64;
     MSVYPSVLEA IGNTPLIRLN AVSEATGCTI LGKAEFLNPG QSVKDRAALW IIREAEKAGQ
     LRPGGVIVEG TAGNTGIGLA VVGSALGYRT VIVIPETQSQ EKKDALRLLG AELVEVPAVP
     YKNPNNYVKI SGRLAAELAK TEPNGAIWAN QFDNVANREA HVQTTAPEIW RDTDGKVDGF
     ICAVGSGGTI AGVAEGLRAK NPAVKIGIAD PEGAALYNYY AHGELKASGS SITEGIGQGR
     VTANLEGFTP DFAYQIPDSE AVPYVFDLIE KEGLCVGGSS GINIAGAVRL ARELGPGHTI
     VTILCDYGNR YQSKLFNPDF LASKGLPVPA WLNKSSNITV PYEPIG
//
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