ID A0A2A5YTU3_9SPHN Unreviewed; 1072 AA.
AC A0A2A5YTU3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:PDH68221.1};
GN ORFNames=CNE89_04480 {ECO:0000313|EMBL:PDH68221.1};
OS Sphingomonadaceae bacterium MED-G03.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae.
OX NCBI_TaxID=1986231 {ECO:0000313|EMBL:PDH68221.1, ECO:0000313|Proteomes:UP000219365};
RN [1] {ECO:0000313|EMBL:PDH68221.1, ECO:0000313|Proteomes:UP000219365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED-G03 {ECO:0000313|EMBL:PDH68221.1};
RA Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA Rodriguez-Valera F.;
RT "Fine stratification of microbial communities through a metagenomic profile
RT of the photic zone.";
RL Submitted (AUG-2017) 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:PDH68221.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NTKY01000010; PDH68221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5YTU3; -.
DR Proteomes; UP000219365; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR011659; PD40.
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 Pfam; PF07676; PD40; 3.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:PDH68221.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1072
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012563035"
FT DOMAIN 975..1040
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 1072 AA; 115384 MW; FF342D5463B8F8BA CRC64;
MRFPTFLMLS AALVAAPSLA AAQTSGLDLQ PTRTLAYAAQ EGTWMQPDMA PDGKTILFDL
LGDIYALDAA GGAARPVLTG MAFERNPVFS PDGTQFAFLS DRSGATNLWV ANADGTGLKQ
LSHDDKVAIY SSPAWSPDGR FISVSRTVHS ILAFELFLYD KDGGSGIQIT KAGSPDNWDE
KMNAMGAVHA PDGRYLYYAT KRGHTWTEND LPNWSIARRD IKTGQDETII QSAGGAMRPA
LSHDGRLIAY ASRSLANGGQ QDGLRLRDLE TGEDKWIAFP IDRDGQDGGY YADLLPRYSF
MPGDKALLIS VRGKLARLDI ATGALTDIPF TTPVKLGLGP LTRVRQKEET GPVRVRVVQA
PRQSPDGRRV AFTALGGLYV QDLAAGAAPR RIVETDAFQP SWSPDGRTIV YVRWTATGGG
HIWSVPASGG TPRRLTQIPA YYTEPVFTPD GGSIVALRAN QHDRLRAVSE IDPSRPTDII
RLPARGGPVA QITHAMGARL PHFAQDGRLL FYSPAGVASV PLSGGDPQIA LRVLAPGLGQ
YFPGPAPVEE VRLSPDMRHA LVKSFSQVYI LDVPPANGAE PPTINLSAPI VAKAKLTRVG
ADFTDWADEG ATVTWSVGST FRRVPTAQAL SAPAQGSEAM AQSYPLPVAL PRDVPQGSIV
LRGATVLPMA GAQPVIANAD IVITDNRIVA VGPSGSVAVP AGASVRDVSG KYIVPGFVDT
HAHWFEIRRG IQERGHWDFA ANLAYGVTSA LDVQPFTSDV FAYQDMIDAG MMVGPRAWST
GPGVFVNAEI HSRQDAIDVL TRYRDHYRTR NIKSYMIGDR AQRQYMVEAA SALGMMPTTE
GASDMVLNLT HAIDGFSGNE HAIPVSPLRQ DIIRLFAQSR TSYTPTILVA YGTTPALFDF
IIHKRPQDDP RFRHFVPPGI VSEKLRNRHW MPPEAQSWRT IAADAVAIQR AGGLVGIGSH
GEMQGLGYQW EMQAFAAGGA TPMETLKAAT IGSAEVIGHS DDVGSLEPGK FADLLILDAD
PLADIANAMK IGAVMKNGRL YDPMTLDEIW PNPRKRPAAW FHGDDAAPTA AP
//
