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Database: UniProt
Entry: A0A0A7PEV6_9SPHN
LinkDB: A0A0A7PEV6_9SPHN
Original site: A0A0A7PEV6_9SPHN 
ID   A0A0A7PEV6_9SPHN        Unreviewed;       544 AA.
AC   A0A0A7PEV6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Amidohydrolase family protein {ECO:0000313|EMBL:AJA07723.1};
GN   ORFNames=SKP52_03975 {ECO:0000313|EMBL:AJA07723.1};
OS   Sphingopyxis fribergensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1515612 {ECO:0000313|EMBL:AJA07723.1, ECO:0000313|Proteomes:UP000030907};
RN   [1] {ECO:0000313|EMBL:AJA07723.1, ECO:0000313|Proteomes:UP000030907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kp5.2 {ECO:0000313|EMBL:AJA07723.1,
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; AJA07723.1; -; Genomic_DNA.
DR   RefSeq; WP_052207776.1; NZ_CP009122.1.
DR   AlphaFoldDB; A0A0A7PEV6; -.
DR   STRING; 1515612.SKP52_03975; -.
DR   KEGG; sphk:SKP52_03975; -.
DR   HOGENOM; CLU_016107_2_1_5; -.
DR   OrthoDB; 9766983at2; -.
DR   Proteomes; UP000030907; Chromosome.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   Gene3D; 3.30.1490.130; D-aminoacylase. Domain 3; 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; IPR013108; Amidohydro_3.
DR   InterPro; IPR023100; D-aminoacylase_insert_dom_sf.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11647:SF1; COLLAPSIN RESPONSE MEDIATOR PROTEIN; 1.
DR   PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR   Pfam; PF07969; Amidohydro_3; 2.
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:AJA07723.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..544
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002031754"
FT   DOMAIN          79..262
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   DOMAIN          411..518
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   544 AA;  57831 MW;  F8D716CA207154FF CRC64;
     MPQPLAPLSV RRTIGSFSLA AALLCVAGAS AKTDEAVDVI IRGGTIYDGG EGKPFVGDVA
     IRGDRIVYVG KSGRHKAGKV IDAKGMIVAP GFIDPHTHAD SFIRSPDKAV RVNAAWLRQG
     ATTVMIGVDG SGTPDVAEDA GKLAASGIGT NIVPFVGFGP VRQRALGQDA RAPNDAELNA
     MKGLVAKGMC EGAVGLSTGL FYAPQSFATT GEVVAVAREA AIRGGIYDTH QRDESSYSIG
     LLGSVKEAIE IGREAGMPVH FAHLKALGVD VHGQAGAVIA AIDAARKAGV DVTADQYPWL
     ASGSSLDASL LPRWAVDGGG PALLKRLDDP ATLARIRAEM QENLRRRGGA SALLLIAQGF
     PWTGKTLAQV ADEWKLDSRD AALRIIRKSI EEKDPERGGG TAVASFNMAQ ADVDLLMKQP
     WMVTSSDGSD GHPRMFATFP EKYVRYVRER KVIDLRAFIR QSTGRTADIY KLDRRGYLRP
     GYFADILVFD PDRYAPRADY VRPRELSVGV RKLFVNGVLA VDDGRTTGAA AGRTLLRSRP
     SGCS
//
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