ID Q1GTR9_SPHAL Unreviewed; 444 AA.
AC Q1GTR9;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ABF52953.1};
GN OrderedLocusNames=Sala_1238 {ECO:0000313|EMBL:ABF52953.1};
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655 {ECO:0000313|EMBL:ABF52953.1, ECO:0000313|Proteomes:UP000006578};
RN [1] {ECO:0000313|EMBL:ABF52953.1, ECO:0000313|Proteomes:UP000006578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256
RC {ECO:0000313|Proteomes:UP000006578};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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DR EMBL; CP000356; ABF52953.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1GTR9; -.
DR STRING; 317655.Sala_1238; -.
DR KEGG; sal:Sala_1238; -.
DR eggNOG; COG1228; Bacteria.
DR HOGENOM; CLU_023620_2_2_5; -.
DR OrthoDB; 9782972at2; -.
DR Proteomes; UP000006578; Chromosome.
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; 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:0000313|EMBL:ABF52953.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006578};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..444
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004189570"
FT DOMAIN 91..441
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 444 AA; 47444 MW; 8FF169F700A036BF CRC64;
MQSRVKLRSF LRVMRIGGIA LLGAVGTGTA AQEAPSQTVI TAARYIDVLS GKTVEHPAIF
VGADGRITNI ADARTVRWGS DVKHIDLGGK TLLPGLIDMH VHLDGPADIG GYRGLEFTDS
FWGMTAVKNA NDMLNAGFTT VRNVGSGDRN DIGLKQAIDS GYATGPRIVP AGYALGATGG
HCDSTFLPPS LEKKDGKEEG IGDSPDELRY QVRRQRKYGA EVIKVCATGG VFSRNTEPGQ
LQVPENELRA IADEAHQWGL RVAAHAHGAA GIRAAIAAGI DTIEHASLVD DEGIRMAVAR
KQPVWFAMDI YNTEYTQAEG SKNGVLEDNL RKDREIAQIQ RDNFRKAHRA GVRMVFASDA
GVMPHGEVGK QFRVMVEYGM TPIQAIQAAT KNAAEALGRE KDVGAIAVGR YADIVAVDGD
PLANVRELES VDAVVKGGVL VKGE
//
