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
//