ID A8F705_PSELT Unreviewed; 450 AA.
AC A8F705;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:ABV33939.1};
GN OrderedLocusNames=Tlet_1382 {ECO:0000313|EMBL:ABV33939.1};
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=416591 {ECO:0000313|EMBL:ABV33939.1, ECO:0000313|Proteomes:UP000002016};
RN [1] {ECO:0000313|EMBL:ABV33939.1, ECO:0000313|Proteomes:UP000002016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC {ECO:0000313|Proteomes:UP000002016};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABV33939.1, ECO:0000313|Proteomes:UP000002016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC {ECO:0000313|Proteomes:UP000002016};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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DR EMBL; CP000812; ABV33939.1; -; Genomic_DNA.
DR RefSeq; WP_012003415.1; NZ_BSDV01000001.1.
DR AlphaFoldDB; A8F705; -.
DR STRING; 416591.Tlet_1382; -.
DR KEGG; tle:Tlet_1382; -.
DR eggNOG; COG1574; Bacteria.
DR HOGENOM; CLU_009942_3_1_0; -.
DR OrthoDB; 9767366at2; -.
DR Proteomes; UP000002016; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.10.310.70; -; 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; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR22642:SF23; AMIDOHYDROLASE YTCJ-RELATED; 1.
DR PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR Pfam; PF07969; Amidohydro_3; 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:ABV33939.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002016}.
FT DOMAIN 34..445
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 450 AA; 51699 MW; 7206EAA8EAF561B5 CRC64;
MIFRNCAVYK NGNFEKSDLF VENGIFTDSS SGPVIDLSGM YVMPGFVDSH AHILGVGQKC
EHLNLEKICS QEELFQLLIK QDKKIILGRG WSEQTLGGYP DKKMLDKIQK PVVLTRKCGH
VAVLNQSAMN LINMYKEDGI FKEDELEKIR GRLNNEDAER LFKIGEEEFL KHGVTFVHSD
DLHGLSWDEL KRILKKSRIR IFEKLHFSRI EDLERFNEFG VLTERVYVKG VKIFADGSLG
GKTAYLSKPY ADEKSYRGMC LANSQQIERF AEICSRKKVQ LCIHAIGDAA VHEVAMALKN
YPKNRLIHAQ LIDEKDLKYL KDTYFCVQPH FAFEDQELIS RRISKEFYGL KYDFLKLFKE
GYRVTFSTDA PVSPHDPKYV IEAALRMGFH LMDAINLYTY ASSETTGLRN IGKIEIGYAA
DFAIYEKNPL KLEDDPIAVY VHGEQIWQKA
//
