ID A4CMR2_ROBBH Unreviewed; 548 AA.
AC A4CMR2;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:EAR14954.1};
GN OrderedLocusNames=RB2501_11527 {ECO:0000313|EMBL:EAR14954.1};
OS Robiginitalea biformata (strain ATCC BAA-864 / HTCC2501 / KCTC 12146).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Robiginitalea.
OX NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR14954.1, ECO:0000313|Proteomes:UP000009049};
RN [1] {ECO:0000313|EMBL:EAR14954.1, ECO:0000313|Proteomes:UP000009049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146
RC {ECO:0000313|Proteomes:UP000009049};
RX PubMed=19767438; DOI=10.1128/JB.01191-09;
RA Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Robiginitalea biformata HTCC2501.";
RL J. Bacteriol. 191:7144-7145(2009).
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DR EMBL; CP001712; EAR14954.1; -; Genomic_DNA.
DR RefSeq; WP_015754275.1; NC_013222.1.
DR AlphaFoldDB; A4CMR2; -.
DR STRING; 313596.RB2501_11527; -.
DR KEGG; rbi:RB2501_11527; -.
DR eggNOG; COG3653; Bacteria.
DR HOGENOM; CLU_016107_2_1_10; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000009049; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR CDD; cd01297; D-aminoacylase; 1.
DR Gene3D; 3.30.1490.130; D-aminoacylase. Domain 3; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
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:SF99; D-PHENYLHYDANTOINASE-RELATED; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009049}.
FT DOMAIN 439..523
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 548 AA; 60832 MW; 2A39C51ACF0BAE44 CRC64;
MYALRFLILL LIFSSCQPEP GFDVVIRGGQ LLDGSGSPAI RADLGIRGDT IAAIGDLSGR
KAKTEIDATG LHLAPGFINM LSWANVSLLE DGRSQSDIRQ GVTLEVLGEG RSMGPLNEEM
KREMRNGQQD ITYDIPWTTL GEYLQHLEER GVSTNVASFV GNGTLREYVM GYEKRAPTPA
EMDSMKTLLR RGMEEGAVGL STSLIYVPSG HASTGEITDL ARVVSEYGGM YISHIRNEED
SLLHAVRELI QIAEDADVPA EIYHFKASGQ DNWDLLDSAI ALVEDARSRG LEITTDMYMY
NASSTGLNVL LPAWAKDGGH ERTMEYLRDP EARQRMIEEV KFHVPPENIL LVGFRNKDMR
HLIGKNLAEV AAERGIRPRE AIADLIFEDD SRIQVVYFSM SEENVEKKLA LPYMAICSDA
GSYTNEGVFL EQSTHPRAYG SFARLLSHFV RDRGVISLEE AVRRLTSLPA GNLKLRGRGQ
LKPGYFADVV VFDPERIQDR ATFEQPHQYA SGVEHVLVNG VPVLQNGEHT GNFPGRFVRG
PGYQMKKP
//
