ID A0A0A7PSN4_9SPHN Unreviewed; 433 AA.
AC A0A0A7PSN4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:AJA11042.1};
GN ORFNames=SKP52_20890 {ECO:0000313|EMBL:AJA11042.1};
OS Sphingopyxis fribergensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1515612 {ECO:0000313|EMBL:AJA11042.1, ECO:0000313|Proteomes:UP000030907};
RN [1] {ECO:0000313|EMBL:AJA11042.1, ECO:0000313|Proteomes:UP000030907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kp5.2 {ECO:0000313|EMBL:AJA11042.1,
RC ECO:0000313|Proteomes:UP000030907};
RX PubMed=26040579; DOI=10.1099/ijs.0.000371;
RA Oelschlagel M., Ruckert C., Kalinowski J., Schmidt G., Schlomann M.,
RA Tischler D.;
RT "Description of Sphingopyxis fribergensis sp. nov. - a soil bacterium with
RT the ability to degrade styrene and phenylacetic acid.";
RL Int. J. Syst. Evol. Microbiol. 65:3008-3015(2015).
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DR EMBL; CP009122; AJA11042.1; -; Genomic_DNA.
DR RefSeq; WP_039578253.1; NZ_CP009122.1.
DR AlphaFoldDB; A0A0A7PSN4; -.
DR STRING; 1515612.SKP52_20890; -.
DR KEGG; sphk:SKP52_20890; -.
DR HOGENOM; CLU_023620_2_2_5; -.
DR OrthoDB; 9782972at2; -.
DR Proteomes; UP000030907; 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:AJA11042.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..433
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002044448"
FT DOMAIN 79..432
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 433 AA; 44721 MW; 479AADD5DE315FC2 CRC64;
MKPIHYLPLA LVGAALASPL AAQAPARTVI HAGQLLAEPG KPVRGASTII VEGGKILSIA
DGYQPADPGA TLIDLKDKYV LPGLIDSHVH LTSDAGGIAG QLEEVTLSPA AQAFNAEANG
MKTLRAGFTT VRNLGDGDGA TLALRDAIAA GKVRGPRIVD AGNSISGSAG HMDGSLGYRD
ELRPFFAGAG NTCNGADDCR RAVRLQIGRG ADVIKFASTG GVNSRIGAGL GKQMFDDEAQ
AIVDTAHLFG KKVAVHAHGA DGIRLAIDAG ADSIEHGTIL DEATIAAWAK SKTYYVPTLS
TVNGYKERLA ANPDAYEPDV LAKIQWRISI TGKSLEQLVP RGVRIAFGTD AGVSKHGRNG
DEFGLMVQHG MKPVEALKAA TVNAADLLGL SDQIGTIAPG KSADIIAVAS DPVADVRVLK
KVDFVMARGA VVD
//
