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Database: UniProt
Entry: U5RSI1_9CLOT
LinkDB: U5RSI1_9CLOT
Original site: U5RSI1_9CLOT 
ID   U5RSI1_9CLOT            Unreviewed;       455 AA.
AC   U5RSI1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:AGY75721.1};
DE            EC=3.5.2.2 {ECO:0000313|EMBL:AGY75721.1};
GN   Name=hydA {ECO:0000313|EMBL:AGY75721.1};
GN   ORFNames=CAETHG_1496 {ECO:0000313|EMBL:AGY75721.1};
OS   Clostridium autoethanogenum DSM 10061.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY75721.1, ECO:0000313|Proteomes:UP000017590};
RN   [1] {ECO:0000313|EMBL:AGY75721.1, ECO:0000313|Proteomes:UP000017590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY75721.1};
RX   PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA   Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA   Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT   "Comparison of single-molecule sequencing and hybrid approaches for
RT   finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT   systems in industrial relevant Clostridia.";
RL   Biotechnol. Biofuels 7:40-40(2014).
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}.
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DR   EMBL; CP006763; AGY75721.1; -; Genomic_DNA.
DR   RefSeq; WP_013240213.1; NZ_CP012395.1.
DR   AlphaFoldDB; U5RSI1; -.
DR   SMR; U5RSI1; -.
DR   KEGG; cah:CAETHG_1496; -.
DR   PATRIC; fig|1341692.11.peg.1504; -.
DR   HOGENOM; CLU_015572_2_0_9; -.
DR   Proteomes; UP000017590; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004157; F:dihydropyrimidinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   InterPro; IPR011612; Urease_alpha_N_dom.
DR   NCBIfam; TIGR02033; D-hydantoinase; 1.
DR   PANTHER; PTHR11647:SF1; COLLAPSIN RESPONSE MEDIATOR PROTEIN; 1.
DR   PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGY75721.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          1..34
FT                   /note="Urease alpha-subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00449"
FT   DOMAIN          49..433
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   MOD_RES         149
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ   SEQUENCE   455 AA;  50670 MW;  6ADE5ED685832D93 CRC64;
     MDLIIKNGVI ITAKDTYKAD IGIKNGKIAV IGKEIEGSGE EIIDAEGKYV LPGAIDAHTH
     LEMPFGGTIS ADSYEAGTRA AACGGTTTVF DFALQQKGHG IIQTARERDE LCAPQACVDY
     AFHVVISDLR PEILDEFQAA VDYGLPSFKV YMVYKKEGLM ADDGVLCQVL EKSKETGALI
     SVHAENPDLI DIRTDKYLKE GKTSAWYHYM SRPEFVEAEA DKRAIHWAKS LNAPLYIVHL
     ANKEGMEEVK RAKDEGYEIY AETCPQYLYF TSEVYKREDG RNFVCSPPMK GKESLDALWK
     GIKTGDISTI ATDHCPFQSS EKDWGKDDFT KIPNGCMGIE NMYPYMLSEA NKGRISFNKA
     VEVCSANPAK IFGCDNQKGS IVIGKDADIV IYDPKKEFTI SKNNMHSDVD YTIWEGVKLK
     GYPVMTLSRG KLVFKDGEFV GKPGWGKFLK RKIKR
//
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