ID A0A0F2J014_9BACT Unreviewed; 302 AA.
AC A0A0F2J014;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=cysteine synthase {ECO:0000256|ARBA:ARBA00012681};
DE EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681};
GN ORFNames=MCHI_003353 {ECO:0000313|EMBL:KJR40745.1};
OS Candidatus Magnetoovum chiemensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Magnetoovum.
OX NCBI_TaxID=1609970 {ECO:0000313|EMBL:KJR40745.1, ECO:0000313|Proteomes:UP000033718};
RN [1] {ECO:0000313|EMBL:KJR40745.1, ECO:0000313|Proteomes:UP000033718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-04 {ECO:0000313|EMBL:KJR40745.1,
RC ECO:0000313|Proteomes:UP000033718};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR605856-50};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2. {ECO:0000256|ARBA:ARBA00004962}.
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:KJR40745.1}.
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DR EMBL; JZJI01000836; KJR40745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2J014; -.
DR PATRIC; fig|1609970.3.peg.3683; -.
DR Proteomes; UP000033718; Unassembled WGS sequence.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; IPR005856; Cys_synth.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01136; cysKM; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF162; CYSTEINE SYNTHASE B; 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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Lyase {ECO:0000313|EMBL:KJR40745.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR605856-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000033718};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..282
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT BINDING 70
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 175..179
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 256
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT MOD_RES 40
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 302 AA; 32789 MW; 62467C066032A2E8 CRC64;
MSVLDAIGNT PIVELKTINP NPKVRLFAKL EGNNPGGSVK DRIAYYMIKD AEDAGDLKKG
QIIFEPTSGN TGIGLAMVGA AKGYKVKLVM PECVSLERRN TLEAFGAELI LSPGKEGTDG
AIRLARKMYE DYKGEYFMPD QFNNPSNIKA HYETTGKEVY EQTKGEVSVF VAGMGTTGTI
MGSGRRLKEY DKSIQIVACE PRLGHKIQGL KNMSESIVPG IFDLSKIDEK RNVDDDIAYN
TARELAVTEG LFVGMSSGAA MAVAIEKIKE MKDGALVVIL PDRGDRYLST TLFKSVCAAC
PP
//
