ID A0A0L6JX81_9FIRM Unreviewed; 406 AA.
AC A0A0L6JX81;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KNY30344.1};
GN ORFNames=Bccel_5624 {ECO:0000313|EMBL:KNY30344.1};
OS Pseudobacteroides cellulosolvens ATCC 35603 = DSM 2933.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudobacteroides.
OX NCBI_TaxID=398512 {ECO:0000313|EMBL:KNY30344.1, ECO:0000313|Proteomes:UP000036923};
RN [1] {ECO:0000313|Proteomes:UP000036923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2933 {ECO:0000313|Proteomes:UP000036923};
RA Dassa B., Utturkar S.M., Klingeman D.M., Hurt R.A., Keller M., Xu J.,
RA Reddy Y.H.K., Borovok I., Grinberg I.R., Lamed R., Zhivin O., Bayer E.A.,
RA Brown S.D.;
RT "Near-Complete Genome Sequence of the Cellulolytic Bacterium Bacteroides
RT (Pseudobacteroides) cellulosolvens ATCC 35603.";
RL Submitted (JUL-2015) 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:KNY30344.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGTC01000001; KNY30344.1; -; Genomic_DNA.
DR RefSeq; WP_036939955.1; NZ_LGTC01000001.1.
DR AlphaFoldDB; A0A0L6JX81; -.
DR STRING; 398512.Bccel_5624; -.
DR eggNOG; COG1228; Bacteria.
DR OrthoDB; 9797498at2; -.
DR Proteomes; UP000036923; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 2.
DR InterPro; IPR006680; Amidohydro-rel.
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; PF01979; Amidohydro_1; 2.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KNY30344.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000036923};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..292
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 334..402
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 406 AA; 44734 MW; 555A73CF0A6894FD CRC64;
MVLRFLTRFM LIILVIILLL GIPGYVYYTL TLYKPKTVQK GYLALTRASV LVGENLNSFM
DSTILIKDGV IVKVGNSSDI TIPEGAATLD MNGCTVMPGL IDMHVHLSSY EHQVNKVLNF
LSMPKMLADL VRFTPDKRQA LLKNGVTSVC SLGDEYKWIM DLKKQIRDGV LEGPRIFAAG
PVFTIPGSHT TDVLGADPES VRLPSTPEEA QRMVRELAHN DEPIDLIKVV QDRGDRQHAL
HPVAHDILHA IVNEAHNHSL PVVARWGTEE DLQDVLDAGV DSLQHLEDHT GDINNLWPDN
ILKLILNHNM PRIVVGTYAG MPGAFFGDGI HHEMEKLVES GLTPREALKA ATSGAAKVLR
TDYIGTIGVG QVADLIVIDG NPLKNIKDTR NIVMVLRDGR IVVDQL
//
