BETC_RHIME
ID BETC_RHIME Reviewed; 512 AA.
AC O69787;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Choline-sulfatase;
DE EC=3.1.6.6;
GN Name=betC; OrderedLocusNames=R00949; ORFNames=SMc00127;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=102F34;
RX PubMed=9141699; DOI=10.1099/00221287-143-4-1369;
RA Pocard J.A., Vincent N., Boncompagni E., Tombras Smith L., Poggi M.-C.,
RA Le Rudulier D.;
RT "Molecular characterization of the bet genes encoding glycine betaine
RT synthesis in Sinorhizobium meliloti 102F34.";
RL Microbiology 143:1369-1379(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [4]
RP CHARACTERIZATION.
RC STRAIN=102F34;
RX PubMed=9736747; DOI=10.1073/pnas.95.19.11394;
RA Oesteras M., Boncompagni E., Vincent N., Poggi M.-C., Le Rudulier D.;
RT "Presence of a gene encoding choline sulfatase in Sinorhizobium meliloti
RT bet operon: choline-O-sulfate is metabolized into glycine betaine.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11394-11399(1998).
CC -!- FUNCTION: Converts choline-O-sulfate into choline.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choline sulfate + H2O = choline + H(+) + sulfate;
CC Xref=Rhea:RHEA:20820, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:16822; EC=3.1.6.6;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amine and polyamine biosynthesis; choline biosynthesis;
CC choline from choline sulfate: step 1/1.
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC residue in eukaryotes, is critical for catalytic activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; U39940; AAC13371.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45521.1; -; Genomic_DNA.
DR RefSeq; NP_385055.1; NC_003047.1.
DR RefSeq; WP_010968942.1; NC_003047.1.
DR PDB; 4UG4; X-ray; 2.79 A; A/B/C/D/E/F/G/H=2-512.
DR PDB; 6FNY; X-ray; 2.79 A; A/B/C/D/E/F/G/H=2-512.
DR PDB; 6G5Z; X-ray; 1.98 A; A/B/C/D=5-512.
DR PDB; 6G60; X-ray; 1.84 A; A/B/C/D=5-512.
DR PDBsum; 4UG4; -.
DR PDBsum; 6FNY; -.
DR PDBsum; 6G5Z; -.
DR PDBsum; 6G60; -.
DR AlphaFoldDB; O69787; -.
DR SMR; O69787; -.
DR STRING; 266834.SMc00127; -.
DR EnsemblBacteria; CAC45521; CAC45521; SMc00127.
DR GeneID; 61602415; -.
DR KEGG; sme:SMc00127; -.
DR PATRIC; fig|266834.11.peg.2348; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_9_1_5; -.
DR OMA; YGWAVNW; -.
DR BioCyc; MetaCyc:MON-223; -.
DR BRENDA; 3.1.6.6; 5347.
DR UniPathway; UPA00290; UER00431.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0047753; F:choline-sulfatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042425; P:choline biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16032; choline-sulfatase; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR017785; Choline-sulfatase.
DR InterPro; IPR025863; Choline_sulf_C_dom.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF12411; Choline_sulf_C; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR TIGRFAMs; TIGR03417; chol_sulfatase; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
DR PROSITE; PS00149; SULFATASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..512
FT /note="Choline-sulfatase"
FT /id="PRO_0000192684"
FT ACT_SITE 54
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 104
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 54
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CONFLICT 430
FT /note="R -> S (in Ref. 1; AAC13371)"
FT /evidence="ECO:0000305"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6G60"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 160..180
FT /evidence="ECO:0007829|PDB:6G60"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 191..203
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 234..242
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 252..282
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:4UG4"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 342..349
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:6G60"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:6G60"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 432..448
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 451..472
FT /evidence="ECO:0007829|PDB:6G60"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:6G60"
FT HELIX 499..506
FT /evidence="ECO:0007829|PDB:6G60"
SQ SEQUENCE 512 AA; 58505 MW; ED7A4340258A6291 CRC64;
MTTGKPNILI IMVDQLNGKL FPDGPADFLH APNLKALAKR SARFHNNYTS SPLCAPARAS
FMAGQLPSRT RVYDNAAEYQ SSIPTYAHHL RRAGYYTALS GKMHFVGPDQ LHGFEERLTT
DIYPADFGWT PDYRKPGERI DWWYHNLGSV TGAGVAEITN QMEYDDEVAF LANQKLYQLS
RENDDESRRP WCLTVSFTHP HDPYVARRKF WDLYEDCEHL TPEVGAIPLD EQDPHSQRIM
LSCDYQNFDV TEENVRRSRR AYFANISYLD EKVGELIDTL TRTRMLDDTL ILFCSDHGDM
LGERGLWFKM NFFEGSARVP LMIAGPGIAP GLHLTPTSNL DVTPTLADLA GISLEEVRPW
TDGVSLVPMV NGVERTEPVL MEYAAEASYA PLVAIREGKW KYVYCALDPE QLFDLEADPL
ELTNLAENPR GPVDQATLTA FRDMRAAHWD MEAFDAAVRE SQARRWVVYE ALRNGAYYPW
DHQPLQKASE RYMRNHMNLD TLEESKRYPR GE
