CREA_PSEPU
ID CREA_PSEPU Reviewed; 403 AA.
AC P38488;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Creatinase;
DE EC=3.5.3.3;
DE AltName: Full=Creatine amidinohydrolase;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=1696320; DOI=10.1016/0022-2836(90)90201-v;
RA Coll M., Knof S.H., Ohga Y., Messerschmidt A., Huber R., Moellering H.,
RA Ruessmann L., Schumacher G.;
RT "Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal
RT structures.";
RL J. Mol. Biol. 214:597-610(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=3221393; DOI=10.1016/0022-2836(88)90586-4;
RA Hoeffken H.W., Knof S.H., Bartlett P.A., Huber R., Moellering H.,
RA Schumacher G.;
RT "Crystal structure determination, refinement and molecular model of
RT creatine amidinohydrolase from Pseudomonas putida.";
RL J. Mol. Biol. 204:417-433(1988).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=creatine + H2O = sarcosine + urea; Xref=Rhea:RHEA:22456,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:57433,
CC ChEBI:CHEBI:57947; EC=3.5.3.3;
CC -!- SUBUNIT: Homodimer.
CC -!- DOMAIN: Each monomer has two clearly defined domains. The small N-
CC terminal domain (AA 1-161) and the large domain (AA 162-403). Each of
CC the two active sites is made by residues of the large domain of one
CC monomer and some residues of the small domain of the other monomer.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. Creatinase subfamily.
CC {ECO:0000305}.
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DR PDB; 1CHM; X-ray; 1.90 A; A/B=2-402.
DR PDBsum; 1CHM; -.
DR AlphaFoldDB; P38488; -.
DR SMR; P38488; -.
DR BRENDA; 3.5.3.3; 5092.
DR EvolutionaryTrace; P38488; -.
DR GO; GO:0016980; F:creatinase activity; IEA:UniProtKB-EC.
DR CDD; cd01090; Creatinase; 1.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR039394; Creatinase_C.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase.
FT CHAIN 1..403
FT /note="Creatinase"
FT /id="PRO_0000079344"
FT ACT_SITE 232
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1CHM"
FT HELIX 21..37
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:1CHM"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1CHM"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1CHM"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:1CHM"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1CHM"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:1CHM"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1CHM"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:1CHM"
FT HELIX 161..184
FT /evidence="ECO:0007829|PDB:1CHM"
FT HELIX 191..209
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1CHM"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:1CHM"
FT HELIX 272..291
FT /evidence="ECO:0007829|PDB:1CHM"
FT HELIX 298..311
FT /evidence="ECO:0007829|PDB:1CHM"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:1CHM"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:1CHM"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:1CHM"
SQ SEQUENCE 403 AA; 45537 MW; 21C2CD808D017EE0 CRC64;
MQMPKTLRIR NGDKVRSTFS AQEYANRQAR LRAHLAAENI DAAIFTSYHN INYYSDFLYC
SFGRPYALVV TEDDVISISA NIDGGQPWRR TVGTDNIVYT DWQRDNYFAA IQQALPKARR
IGIEHDHLNL QNRDKLAARY PDAELVDVAA ACMRMRMIKS AEEHVMIRHG ARIADIGGAA
VVEALGDQVP EYEVALHATQ AMVRAIADTF EDVELMDTWT WFQSGINTDG AHNPVTTRKV
NKGDILSLNC FPMIAGYYTA LERTLFLDHC SDDHLRLWQV NVEVHEAGLK LIKPGARCSD
IARELNEIFL KHDVLQYRTF GYGHSFGTLS HYYGREAGLE LREDIDTVLE PGMVVSMEPM
IMLPEGLPGA GGYREHDILI VNENGAENIT KFPYGPEKNI IRK
