ID E3GN54_9FIRM Unreviewed; 458 AA.
AC E3GN54;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Amidohydrolase-related domain-containing protein {ECO:0000259|Pfam:PF01979};
GN OrderedLocusNames=ELI_2449 {ECO:0000313|EMBL:ADO37431.1};
OS Eubacterium callanderi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=53442 {ECO:0000313|EMBL:ADO37431.1, ECO:0000313|Proteomes:UP000006873};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KIST612;
RA Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H., Chang I.S.,
RA Choi I.-G.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO37431.1, ECO:0000313|Proteomes:UP000006873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIST612 {ECO:0000313|EMBL:ADO37431.1,
RC ECO:0000313|Proteomes:UP000006873};
RX PubMed=21036996; DOI=10.1128/JB.01217-10;
RA Roh H., Ko H.J., Kim D., Choi D.G., Park S., Kim S., Chang I.S., Choi I.G.;
RT "Complete genome sequence of a carbon monoxide-utilizing acetogen,
RT Eubacterium limosum KIST612.";
RL J. Bacteriol. 193:307-308(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PTM: Carbamylation allows a single lysine to coordinate two divalent
CC metal cations. {ECO:0000256|PIRSR:PIRSR611778-50}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family.
CC {ECO:0000256|ARBA:ARBA00008829}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002273; ADO37431.1; -; Genomic_DNA.
DR RefSeq; WP_013380752.1; NZ_JANGDA010000006.1.
DR AlphaFoldDB; E3GN54; -.
DR MEROPS; M38.976; -.
DR GeneID; 68363529; -.
DR KEGG; elm:ELI_2449; -.
DR eggNOG; COG0044; Bacteria.
DR HOGENOM; CLU_015572_2_0_9; -.
DR Proteomes; UP000006873; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01314; D-HYD; 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; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR02033; D-hydantoinase; 1.
DR PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 50..435
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT MOD_RES 150
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ SEQUENCE 458 AA; 50433 MW; C24F7150E1D82417 CRC64;
MKKTIIKGGI LFSSTDTVNA DILVENDKIA QIGQKIEDSE AKIIEAAGKY IFPGFIDPHT
HLDMDTGTVH TADDFVSATK GAVSGGTTTI IDFATQDKGQ SLTEALKNWH GLADNRSSCH
YGFHMAITDW NETTRSELKT MKDSGVTSFK LYMAYDNLRS NDREIFEILE AVKTFGGLVS
MHCENGDLVN ALIAEQKRQG RTSPAAHPLS RPDFVEAEAV NRFLAIAEAA ESPVYVVHLS
TERGLAECLN ARRRGQKVFI ETCPQYLLLD DSCYELEGFE SAKYVFAPPA RKPLDEKALW
EAVGSGIVDT IGSDHCSFNM KGGKDLGKND FSKIPNGMPG VETRPVLMYT FGVCKNKMTL
NQMAAQLSET PAKIFGMYPQ KGALKPGSDA DIVIWDPEYK GTITQKDQYQ NVDYTPYEGV
KTKGRAEVVL LNGEIIVEKG RVIAENKGQY IPRGICQL
//
