ID K9XCN3_9CHRO Unreviewed; 412 AA.
AC K9XCN3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Amidase, hydantoinase/carbamoylase family {ECO:0000313|EMBL:AFZ29849.1};
DE EC=3.5.1.87 {ECO:0000313|EMBL:AFZ29849.1};
GN ORFNames=Glo7428_1278 {ECO:0000313|EMBL:AFZ29849.1};
OS Gloeocapsa sp. PCC 7428.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Gloeocapsa.
OX NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ29849.1, ECO:0000313|Proteomes:UP000010476};
RN [1] {ECO:0000313|EMBL:AFZ29849.1, ECO:0000313|Proteomes:UP000010476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ29849.1,
RC ECO:0000313|Proteomes:UP000010476};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Gloeocapsa sp. PCC 7428.";
RL Submitted (JUN-2012) 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}.
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DR EMBL; CP003646; AFZ29849.1; -; Genomic_DNA.
DR RefSeq; WP_015187725.1; NC_019745.1.
DR AlphaFoldDB; K9XCN3; -.
DR STRING; 1173026.Glo7428_1278; -.
DR KEGG; glp:Glo7428_1278; -.
DR PATRIC; fig|1173026.3.peg.1347; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_024588_6_0_3; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000010476; Chromosome.
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 GO; GO:0050538; F:N-carbamoyl-L-amino-acid hydrolase activity; IEA:UniProtKB-EC.
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:AFZ29849.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010476};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 215..311
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 216
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 276
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 289
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 412 AA; 43945 MW; BA18A1291876B5FD CRC64;
MTVALIPVVN GDRLNRNISQ LAEIGKLPGG GVSRVAFTAE DILARQLVQS WMIEAGMTVQ
IDAAGNIIGT YAGRQENAGA LATGSHIDTV PVAGKFDGVL GVLAGIEVVH VLQENNIRLR
HPIEVIVFTD EENSVLGCKA MAGTAVLDPG CYRRNDGTPI EACLARIGGD WSQLATAKRQ
PGEIAAFVEL HVEQGGVLES TGDDVGVVIG IVGQYRHHVT VTGRPNHAGT TPMNMRKDAL
VAASQIVLAV NKLATETPGE QVATVGYFSV SPNAANIVPA RVDLKIDLRD MSQTHLEDMV
AQIKNQLVDI AAATQTEIEM TQMLHVLPTL AAPDIQAAIA QICQHLGLSY TYLPSRAGHD
AQEIGRFADM GMIFVPSRAG ISHAEDEYTS PEHCTQGANV LLQTFLKLDE IY
//
