ALN_ORYSJ
ID ALN_ORYSJ Reviewed; 507 AA.
AC B9FDB8; Q0J8Y7;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Probable allantoinase;
DE Short=OsALN;
DE EC=3.5.2.5;
GN Name=ALN; OrderedLocusNames=Os04g0680400, LOC_Os04g58390;
GN ORFNames=OsJ_16648;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Catalyzes the conversion of allantoin (5-ureidohydantoin) to
CC allantoate by hydrolytic cleavage of the five-member hydantoin ring.
CC Catalyzes the first step of the ureide allantoin degradation followed
CC by the sequential activity of AAH, UGLYAH and UAH which allows a
CC complete purine breakdown without the intermediate generation of urea
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-allantoin + H2O = allantoate + H(+); Xref=Rhea:RHEA:17029,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15678,
CC ChEBI:CHEBI:17536; EC=3.5.2.5;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation; allantoate
CC from (S)-allantoin: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Allantoinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF16200.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF16200.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL606456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP008210; BAF16200.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000141; EEE61915.1; -; Genomic_DNA.
DR EMBL; AK067234; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; B9FDB8; -.
DR SMR; B9FDB8; -.
DR STRING; 4530.OS04T0680400-01; -.
DR PaxDb; B9FDB8; -.
DR PRIDE; B9FDB8; -.
DR eggNOG; KOG2584; Eukaryota.
DR HOGENOM; CLU_072441_0_0_1; -.
DR BRENDA; 3.5.2.5; 8948.
DR PlantReactome; R-OSA-1119502; Allantoin degradation.
DR UniPathway; UPA00395; UER00653.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; B9FDB8; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004038; F:allantoinase activity; IBA:GO_Central.
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:UniProtKB-UniPathway.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IBA:GO_Central.
DR InterPro; IPR017593; Allantoinase.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR03178; allantoinase; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Purine metabolism; Reference proteome; Zinc.
FT CHAIN 1..507
FT /note="Probable allantoinase"
FT /id="PRO_0000430042"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 195
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT CONFLICT 143
FT /note="P -> L (in Ref. 6; AK067234)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="A -> E (in Ref. 6; AK067234)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="I -> S (in Ref. 6; AK067234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 54741 MW; AC6EBE22038AA7CA CRC64;
MAMAAAKGRV LPLLAVAAAL AAALLYRAPF SKSLGGEGCS LLPHDHFWIA SERVVTLGRV
GPAAVEVKGG LINAIAVGDY RSFLLRRPVV DYGDAVIMPG LIDVHAHLDE PGRAEWEGFS
TGTRAAAAGG ITTLVDMPLN SYPSTVSEET LKLKLDAAKD KLHVDVGFWG GLVPENALNP
SALESLLNAG VLGLKSFMCP SGINDFPMTN STHIEEGLVT LAKYKRPLLI HAERIPDVQN
EDGIDGELDP KAYTTYLKSR PPAWEEAAIK DLQRAMKDTE IGGRSEGAHI HIVHLSDAKT
SLGLLKDAKQ NGARVSVETC PHYLAFSAEE VPDGDTRFKC APPIRDSTNR DNLWEALLDG
HIDMLSSDHS PSAPDLKLME EGNFLRAWGG ISSLQFVLPV TWSHGKKYGI SLNQLASWWS
ERPAMLAGLK KKGAVLPGYR ADIVVWKPEA QFHLDDSHPV YHKHRNISAY LGKQLSGKIL
STFVGGNLVF AEDKHAKAAC GAPILAK
