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
//