ID A0A431U3J2_9BACT Unreviewed; 414 AA.
AC A0A431U3J2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:RTQ50057.1};
GN ORFNames=EJV47_10470 {ECO:0000313|EMBL:RTQ50057.1};
OS Hymenobacter gummosus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1776032 {ECO:0000313|EMBL:RTQ50057.1, ECO:0000313|Proteomes:UP000282184};
RN [1] {ECO:0000313|EMBL:RTQ50057.1, ECO:0000313|Proteomes:UP000282184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 52166 {ECO:0000313|EMBL:RTQ50057.1,
RC ECO:0000313|Proteomes:UP000282184};
RA Nie L.;
RT "Hymenobacter gummosus sp. nov., isolated from a spring.";
RL Submitted (DEC-2018) 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:RTQ50057.1}.
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DR EMBL; RXOF01000005; RTQ50057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A431U3J2; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000282184; 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 Hydrolase {ECO:0000313|EMBL:RTQ50057.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 215..314
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 218
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 278
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 291
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 414 AA; 43925 MW; 6C2C55506752A235 CRC64;
MPTTYAQRAA DIMQRIHELA AISETPGVVT RTFGTPAFVR GRALVQQWMQ QAGLETRIDN
IGNLRGRLRS PRPGAQTFVI GSHIDTVVNA GRFDGPLGVL LGLDLLAQLQ ARQTELPFHL
ELLAFSDEEG VRFHTTYLGS KVLTGAFEPA LLLRPDATGV PLAEAIRQQG GDPAGLPADA
LPAAAWRGYF EVHIEQGPVL WERQVPVALV TAIAGQRRVE LTFRGMAGHA GTVPMPMRQD
ALAGAAEFVL AAEQLATKHG RGLVATVGKL QLPHAASNVI PGEVSCSLDL RSPDETELAA
AYAALQQQAE ALAARRGLTL DWQLIQQTAP VACDAALNQP LSQAIAAAGH EVIALVSGAG
HDAVPVAQVA PATMLFVRCY RGISHNPLEN VEPEDLAAAL QVAEEFLTLL VSAG
//