ID   CSH_ARTSP               Reviewed;         264 AA.
AC   P32400;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=N-carbamoylsarcosine amidase;
DE            EC=3.5.1.59;
DE   AltName: Full=N-carbamoylsarcosine amidohydrolase;
DE            Short=CSHase;
OS   Arthrobacter sp.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1667;
RN   [1]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SEQUENCE REVISION TO 184 AND
RP   232.
RX   PubMed=1381445; DOI=10.1016/0022-2836(92)91056-u;
RA   Romao M.J., Turk D., Gomis-Rueth F.-X., Huber R.;
RT   "Crystal structure analysis, refinement and enzymatic reaction mechanism of
RT   N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0-A
RT   resolution.";
RL   J. Mol. Biol. 226:1111-1130(1992).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF COMPLEX WITH INHIBITORS.
RX   PubMed=8913306; DOI=10.1006/jmbi.1996.0574;
RA   Zajc A., Romao M.J., Turk D., Huber R.;
RT   "Crystallographic and fluorescence studies of ligand binding to N-
RT   carbamoylsarcosine amidohydrolase from Arthrobacter sp.";
RL   J. Mol. Biol. 263:269-283(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + N-carbamoylsarcosine = CO2 + NH4(+) +
CC         sarcosine; Xref=Rhea:RHEA:20057, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57433, ChEBI:CHEBI:57490; EC=3.5.1.59;
CC   -!- COFACTOR:
CC       Name=sulfate; Xref=ChEBI:CHEBI:16189;
CC       Note=Binds 1 sulfate ion per subunit.;
CC   -!- PATHWAY: Amine and polyamine degradation; creatinine degradation;
CC       sarcosine from creatinine: step 3/3.
CC   -!- SUBUNIT: Homotetramer.
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DR   PIR; S28969; S28969.
DR   PDB; 1NBA; X-ray; 2.00 A; A/B/C/D=1-264.
DR   PDBsum; 1NBA; -.
DR   AlphaFoldDB; P32400; -.
DR   SMR; P32400; -.
DR   BioCyc; MetaCyc:MON-11021; -.
DR   UniPathway; UPA00274; UER00397.
DR   EvolutionaryTrace; P32400; -.
DR   GO; GO:0050127; F:N-carbamoylsarcosine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006602; P:creatinine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.850; -; 1.
DR   InterPro; IPR000868; Isochorismatase-like.
DR   InterPro; IPR036380; Isochorismatase-like_sf.
DR   Pfam; PF00857; Isochorismatase; 1.
DR   SUPFAM; SSF52499; SSF52499; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase.
FT   CHAIN           1..264
FT                   /note="N-carbamoylsarcosine amidase"
FT                   /id="PRO_0000079397"
FT   REGION          240..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        177
FT                   /note="Nucleophile"
FT   HELIX           9..33
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   STRAND          43..51
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   HELIX           54..57
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   HELIX           68..84
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   STRAND          89..94
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   HELIX           109..113
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   STRAND          140..150
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   HELIX           155..161
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   STRAND          166..172
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   TURN            174..176
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   HELIX           177..188
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   STRAND          191..195
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   HELIX           196..198
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   STRAND          202..205
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   HELIX           206..217
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   HELIX           224..233
FT                   /evidence="ECO:0007829|PDB:1NBA"
FT   HELIX           237..239
FT                   /evidence="ECO:0007829|PDB:1NBA"
SQ   SEQUENCE   264 AA;  29057 MW;  8A213B555EA5DCDC CRC64;
     MTETSGTFND IEARLAAVLE EAFEAGTSIY NERGFKRRIG YGNRPAVIHI DLANAWTQPG
     HPFSCPGMET IIPNVQRINE AARAKGVPVF YTTNVYRNRD ASSGTNDMGL WYSKIPTETL
     PADSYWAQID DRIAPADGEV VIEKNRASAF PGTNLELFLT SNRIDTLIVT GATAAGCVRH
     TVEDAIAKGF RPIIPRETIG DRVPGVVQWN LYDIDNKFGD VESTDSVVQY LDALPQFEDT
     VPKTLSDPQP EVEAPADPVF AEQH