ID I4D246_DESAJ Unreviewed; 452 AA.
AC I4D246;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Allantoinase {ECO:0000313|EMBL:AFM39870.1};
GN OrderedLocusNames=Desaci_0813 {ECO:0000313|EMBL:AFM39870.1};
OS Desulfosporosinus acidiphilus (strain DSM 22704 / JCM 16185 / SJ4).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=646529 {ECO:0000313|EMBL:AFM39870.1, ECO:0000313|Proteomes:UP000002892};
RN [1] {ECO:0000313|EMBL:AFM39870.1, ECO:0000313|Proteomes:UP000002892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22704 / JCM 16185 / SJ4
RC {ECO:0000313|Proteomes:UP000002892};
RX PubMed=23105050; DOI=10.1128/JB.01392-12;
RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA Ollivier B., Klenk H.P., Spring S., Loy A.;
RT "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT and Desulfosporosinus acidiphilus DSM22704T.";
RL J. Bacteriol. 194:6300-6301(2012).
CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC to dihydroorotate. {ECO:0000256|ARBA:ARBA00002368}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class I DHOase subfamily.
CC {ECO:0000256|ARBA:ARBA00010286}.
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; CP003639; AFM39870.1; -; Genomic_DNA.
DR RefSeq; WP_014825881.1; NC_018068.1.
DR AlphaFoldDB; I4D246; -.
DR STRING; 646529.Desaci_0813; -.
DR KEGG; dai:Desaci_0813; -.
DR eggNOG; COG0044; Bacteria.
DR HOGENOM; CLU_015572_4_2_9; -.
DR OrthoDB; 9765462at2; -.
DR Proteomes; UP000002892; Chromosome.
DR GO; GO:0004038; F:allantoinase activity; IEA:InterPro.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000256; P:allantoin catabolic process; IEA:InterPro.
DR CDD; cd01315; L-HYD_ALN; 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; IPR017593; Allantoinase.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR011612; Urease_alpha_N_dom.
DR NCBIfam; TIGR03178; allantoinase; 1.
DR PANTHER; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF2; ALLANTOINASE; 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.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 2..41
FT /note="Urease alpha-subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00449"
FT DOMAIN 51..432
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 452 AA; 49233 MW; E16CF363540620E3 CRC64;
MFDLVIKNGK VVKTDRVIEA NIGVNNGKIA AIVESGNPLE GKEVIDAQGT YIFPGAIDSH
AHLNDPGYLW REDYAHGTAA AGVGGITTII DMPLQNEPAM TDAQIFAKKI QAVSANAYVD
YCFWGGLVDY NFDKLKELDE KGCIGFKSFI GPVSPDYVSL SIGQAKEALE ILRAFDARAA
FHCEDYSIIK WEEKRAQRKG NNDWQDFLNS RPVIAELIAT QNIIDLAKEL GAKAHICHVS
HPRVAKIIQE AQQEGIDVTA ETCGHYLTFT DQDVINNGSL FKCAPPLREK AAVEEMWEYV
NNGTLSCVAS DHSPCELSEK SEEKHGIFGA WGGISGIQNV MQVVFSEGVV KRGYNPTLLA
RSLSEGPAKV CGIYGKKGAI EVGFDADLVI LDPEKEWEIT PESLHYVNKI SAFVGLKGKG
LPVCTVVRGQ VVAKDGKIVG PKGFGEFVSK LK
//
