ID F7T7Q5_9BURK Unreviewed; 484 AA.
AC F7T7Q5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=D-aminoacylase 2 {ECO:0000313|EMBL:EGP43681.1};
GN ORFNames=AXXA_24985 {ECO:0000313|EMBL:EGP43681.1};
OS Achromobacter insuavis AXX-A.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1003200 {ECO:0000313|EMBL:EGP43681.1, ECO:0000313|Proteomes:UP000004853};
RN [1] {ECO:0000313|EMBL:EGP43681.1, ECO:0000313|Proteomes:UP000004853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AXX-A {ECO:0000313|EMBL:EGP43681.1,
RC ECO:0000313|Proteomes:UP000004853};
RA Bador J., Amoureux L., Neuwirth C.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGP43681.1}.
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DR EMBL; AFRQ01000114; EGP43681.1; -; Genomic_DNA.
DR RefSeq; WP_006394968.1; NZ_GL982453.1.
DR AlphaFoldDB; F7T7Q5; -.
DR PATRIC; fig|1003200.3.peg.4944; -.
DR eggNOG; COG3653; Bacteria.
DR HOGENOM; CLU_016107_2_0_4; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000004853; Unassembled WGS sequence.
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; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
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; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 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;
FT DOMAIN 53..248
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT DOMAIN 319..464
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 484 AA; 52443 MW; 5CD53DA4B116295C CRC64;
MTASESQPFD YLFVGGTVID GANTPGRRAD LGVRGDRIAA IGDLSGAAAR HRIDVSGQVL
VPGFIDSHTH DDNYLLKRRD MTPKISQGVT TVVTGNCGIS LAPLAHANPP APLDLLDEGG
SYHFKRFADY LEALRATPAA VNAACMVGHS TLRAAVMPDL QRAATDDEID AMRALAEEAM
ASGAIGISTG AFYPPAARAT TEEIIEVCRP LSTHGGIYAT HMRDEGEHIV AALEETFRIG
RELDVPVVIS HHKVMGQPNF GRSRETLPLI EAAMARQDVS LDAYPYVAGS TMLKQDRVLL
AGRTIITWCK PFPELSGRDL DEVAAERGKS KYDVVPELQP AGAIYFMMDE PDVQRILAFG
PTMIGSDGLP HDERPHPRLW GTFPRVLGHY ARDLGLFPLE TAVWKMTGLT AERFGLAERG
QLRPGYFADL VVFDPATVAD TATFERPTER AAGIHSVYVN GVPVWREQAF TGEHAGRVLA
RTPA
//
