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Database: UniProt
Entry: R5BQ97_9FIRM
LinkDB: R5BQ97_9FIRM
Original site: R5BQ97_9FIRM 
ID   R5BQ97_9FIRM            Unreviewed;       200 AA.
AC   R5BQ97;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Amidase {ECO:0000313|EMBL:CCX54907.1};
GN   ORFNames=BN814_00148 {ECO:0000313|EMBL:CCX54907.1};
OS   Veillonella sp. CAG:933.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=1262980 {ECO:0000313|EMBL:CCX54907.1, ECO:0000313|Proteomes:UP000018347};
RN   [1] {ECO:0000313|EMBL:CCX54907.1, ECO:0000313|Proteomes:UP000018347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:933 {ECO:0000313|Proteomes:UP000018347};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M20 family.
CC       {ECO:0000256|ARBA:ARBA00006153}.
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:CCX54907.1}.
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DR   EMBL; CAWP010000090; CCX54907.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5BQ97; -.
DR   Proteomes; UP000018347; Unassembled WGS sequence.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR010158; Amidase_Cbmase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR   PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
FT   DOMAIN          2..103
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   200 AA;  21854 MW;  548ACDED2266D48A CRC64;
     MKGISWQRIE IKGVANHAGT TPTNMRVDAG LAAAKVITFM RDRCNQSGGT TVATTGTIAF
     EPNAINVIPS KAVFTVDVRN PNEERLIAEE QALAAYLKEL AVTDKVQIST EQLVRFQPVQ
     FDETIVSMVE QVANEMHLSN RRMTSGAGQD AQMMARICPS AMIFVPSVNG ISHNPKEYTK
     DEDIFAGANV FINVIKNLAQ
//
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