ID A0A074KX56_9BACT Unreviewed; 429 AA.
AC A0A074KX56;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KEO74556.1};
GN ORFNames=EL17_02460 {ECO:0000313|EMBL:KEO74556.1};
OS Anditalea andensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Anditalea.
OX NCBI_TaxID=1048983 {ECO:0000313|EMBL:KEO74556.1, ECO:0000313|Proteomes:UP000027821};
RN [1] {ECO:0000313|EMBL:KEO74556.1, ECO:0000313|Proteomes:UP000027821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY1 {ECO:0000313|EMBL:KEO74556.1,
RC ECO:0000313|Proteomes:UP000027821};
RA Yang L., Wei S., Tay Q.X.M.;
RT "Characterization and application of a salt tolerant electro-active
RT bacterium.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEO74556.1}.
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DR EMBL; JMIH01000014; KEO74556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074KX56; -.
DR STRING; 1048983.EL17_02460; -.
DR eggNOG; COG1228; Bacteria.
DR OrthoDB; 9797498at2; -.
DR Proteomes; UP000027821; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01299; Met_dep_hydrolase_A; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 2.
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:0000313|EMBL:KEO74556.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027821};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..429
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001697110"
FT DOMAIN 75..424
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT REGION 157..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 46371 MW; 17D4781AF84A0BAB CRC64;
MNHKYLFATI SFGFLFNLSM AQNTYIHAGK FVDVRENRLL DTMTIIIDED IILAVEKGFI
KGNPGDKVID LRRYTVMPGL MDMHVHIESQ TSPNQFAERM TSNEADIAYN AAGYAETTLM
SGFTTVRDLG GSGVNISLKH AIAAGKVVGP RIYTAGKSIA PTGGHADPTN GLKRSMMGDP
GPTDGVINGE SDSRKAVRHQ VKLGADLIKI TATGGVLSVA RDGSAPQFQQ DEINAVIQTA
KDFGIHVAAH AHGDEGMKRA IAGGIHSIEH GTMMSEATMQ LMISQNTWYV PTITAGMSAA
AYARIPGYYH PLVKAKAETI GAQIQTTFEK AYQRGVKIAF GTDAGVFPHG ENYREFIYMT
EVGMPNLEAI QTATLRGAEL LGLVDKVGVL EAGMWADIIA VDGNPEMDIQ VMKEVVFVMK
SGRIYKNEP
//
