ID K9QYE2_NOSS7 Unreviewed; 568 AA.
AC K9QYE2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=N-acyl-D-aspartate/D-glutamate deacylase {ECO:0000313|EMBL:AFY50448.1};
GN OrderedLocusNames=Nos7524_4704 {ECO:0000313|EMBL:AFY50448.1};
OS Nostoc sp. (strain ATCC 29411 / PCC 7524).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=28072 {ECO:0000313|EMBL:AFY50448.1, ECO:0000313|Proteomes:UP000010378};
RN [1] {ECO:0000313|Proteomes:UP000010378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29411 / PCC 7524 {ECO:0000313|Proteomes:UP000010378};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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DR EMBL; CP003552; AFY50448.1; -; Genomic_DNA.
DR RefSeq; WP_015140858.1; NC_019684.1.
DR AlphaFoldDB; K9QYE2; -.
DR STRING; 28072.Nos7524_4704; -.
DR KEGG; nop:Nos7524_4704; -.
DR PATRIC; fig|28072.8.peg.5153; -.
DR eggNOG; COG3653; Bacteria.
DR HOGENOM; CLU_016107_1_0_3; -.
DR OrthoDB; 9802793at2; -.
DR Proteomes; UP000010378; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01297; D-aminoacylase; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000010378}.
FT DOMAIN 44..197
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT DOMAIN 457..546
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 568 AA; 63515 MW; 66DEACF26A1717A6 CRC64;
MLDLLIQNGL IFDGLGSVPV RGDVGIQNGQ IVTIAPSLNI PAREVVDASG LWVTPGFIDI
HTHYDLEVEI APGLGESVRH GVTSVVIGNC SLSIAIGEPQ MLADIFQRVE TLSHRLIAKW
LQTSVSWQTP AEYLQHLQQL PLGANIAPLL GHSALRAEVM GLERSLKVQP SKFELNVMQR
IAADALDAGF VGVSIDMFPW HRMSGEWRGY TIPSQHAKFK EYAMLADLCR RRDRVFQVTP
NLQRLASFLD ILRMGVGIGK RPLRLTVLSA LDAVHDRNLW KVFSPILNIW NHLLGGNVRF
QTLTEPFTIY SDGCVTPLFE EFSTGAQLNG CDSRQERQKL WQSPGFRRQF RQEWLNKRRK
SFHRDLDLME VVQSPQASWE GLSFAEIARQ HQQEPIDFFI EALQEYDTDL RWVATGANDR
LQPRLALMQH PYILPGFTDA GAHVRNLGYY DGALSLLKQA VTTKFMSPEA AIYRVTGEPA
QWFRLDTGVL KVGAKADIVL LDPSALNQPI SPQMEILDPV LDGEPRMVKR GSDEIVTTVY
INGVQVVDQG KVSDRLGCEK LGTVLSPC
//
