ID F7NKP1_9FIRM Unreviewed; 539 AA.
AC F7NKP1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:EGO63345.1};
GN ORFNames=ALO_13299 {ECO:0000313|EMBL:EGO63345.1};
OS Acetonema longum DSM 6540.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Acetonema.
OX NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO63345.1, ECO:0000313|Proteomes:UP000003240};
RN [1] {ECO:0000313|EMBL:EGO63345.1, ECO:0000313|Proteomes:UP000003240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO63345.1,
RC ECO:0000313|Proteomes:UP000003240};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(2011).
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:EGO63345.1}.
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DR EMBL; AFGF01000119; EGO63345.1; -; Genomic_DNA.
DR RefSeq; WP_004096518.1; NZ_AFGF01000119.1.
DR AlphaFoldDB; F7NKP1; -.
DR STRING; 1009370.ALO_13299; -.
DR eggNOG; COG3653; Bacteria.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000003240; 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; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 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:EGO63345.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003240}.
FT DOMAIN 44..99
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT DOMAIN 433..522
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 539 AA; 59229 MW; AD964CCF3FB79FFF CRC64;
MLDLKIINGK IIDGSGKAAY AGDIGIMKDK IAAIGDLSEQ ESVKTVNANG NVVAPGFIDM
HTHSDLSFKY DRQASSKLYS GVTTEVIGNC GIGVAPVREE NRKLLIDYLG TRLIGSIPVN
LELPWTSFSE YLSWFASNPP SINLAPLLGQ GVVRIAVMGF AKGMPNAGEL KDMQQVTDTA
MSEGALGLST GLVYLPGEYS SKEEIAELCK MMIPYRGIYC THMRTESDGI MDAIDEALWI
GGTGGVPVHI SHLKLLSQNM LGKTDLVLER MEKAERSGIE VSYDIYPYTA GLTSLSACLP
PWIFEGGVDK MIARLKDQSV RDRIRQEIAQ GLPGWQNFVK SAGGWEKFFV SSVRSEENKK
LEGKFITEIG EMQGKDPYDA AFDLLIAENG RVQMNYYAMA EEDVMTFLRQ PRAMIGSDAM
SLSTEGILSF GKPHPRAFGT PTRLLGRYVR EKKVLSLEEA IRKMTSLPAQ RLGLNSRGLI
QEGYYADVVI FNPDTVEDRA TYIDPKQHSR GIEAVIVNGQ VILENGSQRK VFAGRILGR
//
