ID G0IUM1_CYCMS Unreviewed; 417 AA.
AC G0IUM1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:AEL24784.1};
GN OrderedLocusNames=Cycma_1012 {ECO:0000313|EMBL:AEL24784.1};
OS Cyclobacterium marinum (strain ATCC 25205 / DSM 745 / LMG 13164 / NCIMB
OS 1802) (Flectobacillus marinus).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=880070 {ECO:0000313|EMBL:AEL24784.1, ECO:0000313|Proteomes:UP000001635};
RN [1] {ECO:0000313|Proteomes:UP000001635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25205 / DSM 745 / LMG 13164 / NCIMB 1802
RC {ECO:0000313|Proteomes:UP000001635};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Cyclobacterium marinum DSM 745.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002955; AEL24784.1; -; Genomic_DNA.
DR RefSeq; WP_014019081.1; NC_015914.1.
DR AlphaFoldDB; G0IUM1; -.
DR STRING; 880070.Cycma_1012; -.
DR KEGG; cmr:Cycma_1012; -.
DR eggNOG; COG3964; Bacteria.
DR HOGENOM; CLU_036699_2_0_10; -.
DR Proteomes; UP000001635; Chromosome.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR020043; Deacetylase_Atu3266-like.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR42717; DIHYDROOROTASE-RELATED; 1.
DR PANTHER; PTHR42717:SF1; DIHYDROOROTASE-RELATED; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF039004; ADE_EF_0837; 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:AEL24784.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001635};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR039004-1}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..417
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003400624"
FT DOMAIN 294..370
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT MOD_RES 189
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ SEQUENCE 417 AA; 45697 MW; A46A424236C12045 CRC64;
MNNFIKLTFT IALLAICSLQ VMGQQYDLLI KGGHVIDAKN NIDEPMDIAI KGDKIALVQK
SIEEDLATQV IDATGLFVSP GLIDIHTHNF YGLDKRGQYS NGYSAIHPDG FTLPYGVTTV
VDAGGSGWRN FIQFKEQVID RVRTRVFAML NIVGHGMKGA LYEQNLDDMD PKMAALVAKQ
FPDHIVGFKV AHYAGHQWQQ IDRLVQAGEL ADIPVMVDFG GANPPLSLET LFMEKLRPGD
IYTHIYGGGG FGRQALVDPA GRLRPFIKAA QERGIIFDVG HGGSSFAFKH AIPSMQQGIK
PNTISTDSHM SSIMSGMKNM TNVMSKFLNM GMNMQEIIAA STWKPAQVIN HTELGHLSEG
AIADIAILNV LEGNFGFTEK TGVGKMMGKY KIENELTIKS GKVVWDLNGL TAPLWDE
//
