RUTD_ECOSE
ID RUTD_ECOSE Reviewed; 266 AA.
AC B6I985;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Putative carbamate hydrolase RutD {ECO:0000255|HAMAP-Rule:MF_00832};
DE EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_00832};
DE AltName: Full=Aminohydrolase {ECO:0000255|HAMAP-Rule:MF_00832};
GN Name=rutD {ECO:0000255|HAMAP-Rule:MF_00832}; OrderedLocusNames=ECSE_1071;
OS Escherichia coli (strain SE11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=409438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SE11;
RX PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT "Complete genome sequence and comparative analysis of the wild-type
RT commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL DNA Res. 15:375-386(2008).
CC -!- FUNCTION: Involved in pyrimidine catabolism. May facilitate the
CC hydrolysis of carbamate, a reaction that can also occur spontaneously.
CC {ECO:0000255|HAMAP-Rule:MF_00832}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamate + 2 H(+) = CO2 + NH4(+); Xref=Rhea:RHEA:15649,
CC ChEBI:CHEBI:13941, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:28938; Evidence={ECO:0000255|HAMAP-Rule:MF_00832};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Hydrolase RutD
CC family. {ECO:0000255|HAMAP-Rule:MF_00832}.
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DR EMBL; AP009240; BAG76595.1; -; Genomic_DNA.
DR RefSeq; WP_000777653.1; NC_011415.1.
DR PDB; 3V48; X-ray; 2.10 A; A/B=1-266.
DR PDBsum; 3V48; -.
DR AlphaFoldDB; B6I985; -.
DR SMR; B6I985; -.
DR ESTHER; ecoli-rutD; RutD.
DR EnsemblBacteria; BAG76595; BAG76595; ECSE_1071.
DR KEGG; ecy:ECSE_1071; -.
DR HOGENOM; CLU_020336_50_1_6; -.
DR OMA; HAMSVTD; -.
DR Proteomes; UP000008199; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0019740; P:nitrogen utilization; IEA:UniProtKB-UniRule.
DR GO; GO:0006212; P:uracil catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00832; RutD; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR019913; Pyrimidine_utilisation_RutD.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR03611; RutD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase.
FT CHAIN 1..266
FT /note="Putative carbamate hydrolase RutD"
FT /id="PRO_0000402944"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3V48"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:3V48"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:3V48"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:3V48"
FT HELIX 63..76
FT /evidence="ECO:0007829|PDB:3V48"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:3V48"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:3V48"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3V48"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:3V48"
FT HELIX 119..148
FT /evidence="ECO:0007829|PDB:3V48"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:3V48"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:3V48"
FT HELIX 175..187
FT /evidence="ECO:0007829|PDB:3V48"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:3V48"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3V48"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:3V48"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3V48"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:3V48"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:3V48"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:3V48"
FT HELIX 244..265
FT /evidence="ECO:0007829|PDB:3V48"
SQ SEQUENCE 266 AA; 28898 MW; 378E13994425E9E2 CRC64;
MKLSLSPPPY ADAPVVVLIS GLGGSGSYWL PQLAVLEQEY QVVCYDQRGT GNNPDTLAED
YSIAQMAAEL HQALVAAGIE HYAVVGHALG ALVGMQLALD YPASVTVLIS VNGWLRINAH
TRRCFQVRER LLYSGGAQAW VEAQPLFLYP ADWMAARAPR LEAEDALALA HFQGKNNLLR
RLNALKRADF SHHADRIRCP VQIICASDDL LVPTACSSEL HAALPDSQKM VMPYGGHACN
VTDPETFNAL LLNGLASLLH HREAAL