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Database: UniProt
Entry: B8FP90_DESHD
LinkDB: B8FP90_DESHD
Original site: B8FP90_DESHD 
ID   B8FP90_DESHD            Unreviewed;       386 AA.
AC   B8FP90;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ACL19615.1};
GN   OrderedLocusNames=Dhaf_1565 {ECO:0000313|EMBL:ACL19615.1};
OS   Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL19615.1, ECO:0000313|Proteomes:UP000007726};
RN   [1] {ECO:0000313|EMBL:ACL19615.1, ECO:0000313|Proteomes:UP000007726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10664 / DCB-2 {ECO:0000313|Proteomes:UP000007726};
RX   PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA   Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA   Tiedje J.M.;
RT   "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT   anaerobe capable of dehalogenation and metal reduction.";
RL   BMC Microbiol. 12:21-21(2012).
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DR   EMBL; CP001336; ACL19615.1; -; Genomic_DNA.
DR   RefSeq; WP_015943515.1; NC_011830.1.
DR   AlphaFoldDB; B8FP90; -.
DR   KEGG; dhd:Dhaf_1565; -.
DR   HOGENOM; CLU_046987_0_0_9; -.
DR   OMA; AWNWEDA; -.
DR   Proteomes; UP000007726; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01309; Met_dep_hydrolase_C; 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; 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; 1.
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:ACL19615.1}.
FT   DOMAIN          226..369
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   386 AA;  41769 MW;  8670D8C919506C29 CRC64;
     MLLIKNGTLL TMTGEPIENG QLLVDKGRII AVGKDLSIPE HCPTLDAEGG FIMPGMIDAH
     CHAGMWEDGL DFEGADGNEG TDPATPHLRA IDAINPRDRA LTEAYEHGVT CICTGPGSAN
     VIGGQFATIK TKGTRIDKMI LQETAAMKVA FGENPKKRYS AKQQSPSTRM ATAAIWREYL
     FKTKNYLENK EKGSGFDLKL ESLIPVVKGE LNVKAHVHRA DDIFTAIRIA KEFGLKMTLE
     HCTEGHLIAD ELAEEGFSVI AGPFIGPRGK VELKELTFAT PAILHKAGLK IALMTDHPVV
     PVHYLPVCAA LAVKAGLAEE TALKAITLNP AEILGISERV GSLEAGKDAD IAVFDRHPLD
     VQAQTTWVLI DGEVVFKRGY FGDSQR
//
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