ID Q97DY8_CLOAB Unreviewed; 393 AA.
AC Q97DY8;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Predicted amidohydrolase (Dihydroorothase family) {ECO:0000313|EMBL:AAK81264.1};
GN OrderedLocusNames=CA_C3332 {ECO:0000313|EMBL:AAK81264.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK81264.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK81264.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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DR EMBL; AE001437; AAK81264.1; -; Genomic_DNA.
DR PIR; E97309; E97309.
DR RefSeq; NP_349924.1; NC_003030.1.
DR AlphaFoldDB; Q97DY8; -.
DR STRING; 272562.CA_C3332; -.
DR DNASU; 1119514; -.
DR KEGG; cac:CA_C3332; -.
DR PATRIC; fig|272562.8.peg.3512; -.
DR eggNOG; COG1228; Bacteria.
DR HOGENOM; CLU_046987_0_0_9; -.
DR OrthoDB; 9802793at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01309; Met_dep_hydrolase_C; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000814}.
FT DOMAIN 55..385
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 393 AA; 43343 MW; E7190D3F2C3935D5 CRC64;
MKKAMLLIKN GKILTMTGVN YDSGSVLIDN GKIIKVGENI DVDESCEIID ADGFWVMPGI
IEAHCHVGIQ EEKRGFEGND CNEMTNPVTP YLRALDGINP MDSAFYTALT AGITGIMVGP
GSANVVGGQW MFLKTYGRAI DKMVVLQPSA MKIAFGENPK ANYDKKNMMP STRIAIAAML
REELFEAQQY YEKRKNAEKS GDSFNKEFRK ECWVPVFDKK IPLKAHVHRA DDILTAIRIA
KEFNLNLTLD HCTEGHLVAK EIKESGFPAI VGPTLTSRNK IETQYADFKT AGILHNEGVK
VAITTDHPVT RIQDLLICAG LAAKEGLGIE EGLKAITINP AEICNVANRV GSIEVNKDAD
IAIFDGNPME TFTKTMYTII NGEIVYSLKD KNY
//
