ID F2RLJ3_STRVP Unreviewed; 525 AA.
AC F2RLJ3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Putative D-aminoacylase {ECO:0000313|EMBL:CCA57952.1};
GN OrderedLocusNames=SVEN_4666 {ECO:0000313|EMBL:CCA57952.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA57952.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA57952.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
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DR EMBL; FR845719; CCA57952.1; -; Genomic_DNA.
DR RefSeq; WP_015035853.1; NZ_JABVZO010000578.1.
DR AlphaFoldDB; F2RLJ3; -.
DR STRING; 953739.SVEN_4666; -.
DR GeneID; 69866744; -.
DR KEGG; sve:SVEN_4666; -.
DR PATRIC; fig|953739.5.peg.7170; -.
DR eggNOG; COG3653; Bacteria.
DR HOGENOM; CLU_016107_2_1_11; -.
DR OMA; HATMNFG; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000006854; 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; IPR013108; Amidohydro_3.
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; 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:UP000006854}.
FT DOMAIN 49..507
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 525 AA; 56650 MW; C219C6B54D8E0B7E CRC64;
MDLVFHDAEV VDGTGGPSYR ADVAVDGGRI AAIVKEGAAA GCQRPTARRV VDAEGLVLSP
GFIDMHAHSD LALLRDPDHS AKAAQGVTLE VLGQDGLSYA PVDDRTLAEV RKAITGWNGS
GDDIDFDWRT VGEYLDRLDR GIAVNAAYLI PQGTVRMYAV GWDDRPATEA ELDHMRRLVA
EGMEQGAVGM SSGLTYTPGM YAKDAELTEL CKVVAGYGGY YCPHHRSYGA GALEAYQEMV
TLTREAGCAL HLAHATMNFG VNEGRAPELL ALLDEALDGG ADISLDTYPY TPGCTTLVAV
LPSWASEGGP EAVLARLRDD ATAERIRHHL EVIGSDGCHG VPMDWDTIEV SGVSEAALTD
WVGRRVDGWE SARRLLLEDR LGTTILQHVG HEENVRTIMR HRVHTGGSDG ILQGLKPHPR
AYGTFPRYLG RYVRELGVLS LEECVAHLTS RPAARLRLPD RGVVREGHIA DLVLFDPETV
GAGATYESPR TLPTGIPHVL VNGEFVVEDG KRTSALAGRS VRRAR
//