ID H3SKV3_9BACL Unreviewed; 406 AA.
AC H3SKV3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:EHQ60298.1};
GN ORFNames=PDENDC454_20937 {ECO:0000313|EMBL:EHQ60298.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ60298.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ60298.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ60298.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(2012).
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:EHQ60298.1}.
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DR EMBL; AHKH01000076; EHQ60298.1; -; Genomic_DNA.
DR RefSeq; WP_006678678.1; NZ_AHKH01000076.1.
DR AlphaFoldDB; H3SKV3; -.
DR STRING; 1131935.PDENDC454_20937; -.
DR PATRIC; fig|1131935.3.peg.4358; -.
DR OrthoDB; 9815027at2; -.
DR Proteomes; UP000003900; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01293; Bact_CD; 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; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR32027:SF9; BLL3847 PROTEIN; 1.
DR PANTHER; PTHR32027; CYTOSINE DEAMINASE; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
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:EHQ60298.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003900}.
FT DOMAIN 205..354
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 406 AA; 44281 MW; B12E096EA010EA45 CRC64;
MYSEYWLTHV RLETGYTKEE GRITGTSTSL FHIRIKEGIM EEIRPAASLP ADPLPRIDAQ
GLLLLPPFRE MHIHLDKTYY GGPWKAVRPV SSIFERIEEE RRLLVEQAPY VKERAAHILD
LILRNGSTHL RAHVNIDPVS ELRNLEKCLE VLEAYRDMLT YEIVGFTQHG LLRSNVSGLL
RQAARSGAGF IGSVDPHSVD GDMKQSLATL MDIAVETNTG IDIHVHDAGE HGLATLHYLA
DLTEDAGWQG RVAVSHSFAF ASASPEEAAE LADRFAALGI AVHSTVPIGR RVMPLPMLKE
RGVPVGLGTD SLTDHWSPFG TGDMLEKAGR LAELYGYSHE HGLSQALGYI TGGVTPLNPD
GQQVWPAPGV PAGGVLVHAS CSAEAVARKS MRQAVLHQGR IVAGSL
//
