ID F4XH38_9FIRM Unreviewed; 395 AA.
AC F4XH38;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=HMPREF0866_02939 {ECO:0000313|EMBL:EGJ45677.1};
OS Ruminococcaceae bacterium D16.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=552398 {ECO:0000313|EMBL:EGJ45677.1, ECO:0000313|Proteomes:UP000002801};
RN [1] {ECO:0000313|Proteomes:UP000002801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D16 {ECO:0000313|Proteomes:UP000002801};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Sibley C.D., White A.P., Crowley S., Surette M.G., Strauss J.C.,
RA Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Clostridium sp. D5.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EGJ45677.1, ECO:0000313|Proteomes:UP000002801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D16 {ECO:0000313|EMBL:EGJ45677.1,
RC ECO:0000313|Proteomes:UP000002801};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., White A.P.,
RA Crowley S., Surette M.G., Strauss J.C., Ambrose C.E., Allen-Vercoe E.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Ruminococcaceae bacterium D16.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001235-1};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR001235-
CC 1};
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:EGJ45677.1}.
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DR EMBL; ADDX02000003; EGJ45677.1; -; Genomic_DNA.
DR AlphaFoldDB; F4XH38; -.
DR STRING; 552398.HMPREF0866_02939; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_024588_6_0_9; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000002801; Unassembled WGS sequence.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03884; M20_bAS; 1.
DR Gene3D; 3.30.70.360; -; 1.
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 NCBIfam; TIGR01879; hydantase; 1.
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 PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002801};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 197..296
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 202
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 262
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 275
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 395 AA; 43276 MW; 731494DB5BA48833 CRC64;
MCEINGERLL SRIQTLGRIG FQDKTGTTRL SYSPEYQEGR RLVEGWMREA GLQTQVDPVG
NLTGRTPGKG PRLCIGSHLD TVPGGGMYDG AYGVLAGIEC VQSLKEAGYA SRRPLEVVGF
IEEEGNVIGG TFGSKAFAGV PVDAAMEPNM AQHGLTPEQV SASRRRGQDY RCYLELHIEQ
GGTLEQEGLQ IGIAHGIVGI LRYRMRVEGF ANHAGSTAMS LRDDALVKTC RMIPWLMDRV
TETSPELVCT VGTLQVFPGA VNVIPGRVEF IVELRGPRME VMDRLIQAFF QQFQAQGLTG
EEYIRQSPTL CSPALIEESR RLCQALNFSS RDMFSGAGHD LINMAQITPS MLLFIPSRKG
ISHSIQEYSA PADLVRGARL LLELVKTLDQ KEGAL
//
