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Probable allantoate deiminase (EC 3.5.3.9) (Allantoate amidohydrolase) (OsAAH)

 AAH_ORYSJ               Reviewed;         491 AA.
Q655X8; A0A0P0WZU4; B9FQD8;
18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
25-OCT-2004, sequence version 1.
30-AUG-2017, entry version 96.
RecName: Full=Probable allantoate deiminase;
EC=3.5.3.9;
AltName: Full=Allantoate amidohydrolase;
Short=OsAAH;
Flags: Precursor;
Name=AAH; OrderedLocusNames=Os06g0665500, LOC_Os06g45480;
ORFNames=OsJ_22281, P0473H04.24;
Oryza sativa subsp. japonica (Rice).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
NCBI_TaxID=39947;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=16100779; DOI=10.1038/nature03895;
International rice genome sequencing project (IRGSP);
"The map-based sequence of the rice genome.";
Nature 436:793-800(2005).
[2]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=18089549; DOI=10.1093/nar/gkm978;
The rice annotation project (RAP);
"The rice annotation project database (RAP-DB): 2008 update.";
Nucleic Acids Res. 36:D1028-D1033(2008).
[3]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=24280374; DOI=10.1186/1939-8433-6-4;
Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H.,
McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
Buell C.R., Matsumoto T.;
"Improvement of the Oryza sativa Nipponbare reference genome using
next generation sequence and optical map data.";
Rice 6:4-4(2013).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H.,
Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
Samudrala R., Wang J., Wong G.K.-S., Yang H.;
"The genomes of Oryza sativa: a history of duplications.";
PLoS Biol. 3:266-281(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Nipponbare;
PubMed=12869764; DOI=10.1126/science.1081288;
The rice full-length cDNA consortium;
"Collection, mapping, and annotation of over 28,000 cDNA clones from
japonica rice.";
Science 301:376-379(2003).
[6]
IDENTIFICATION.
PubMed=19935661; DOI=10.1038/nchembio.265;
Werner A.K., Romeis T., Witte C.P.;
"Ureide catabolism in Arabidopsis thaliana and Escherichia coli.";
Nat. Chem. Biol. 6:19-21(2010).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=23940254; DOI=10.1104/pp.113.224261;
Werner A.K., Medina-Escobar N., Zulawski M., Sparkes I.A., Cao F.Q.,
Witte C.P.;
"The ureide-degrading reactions of purine ring catabolism employ three
amidohydrolases and one aminohydrolase in Arabidopsis, soybean, and
rice.";
Plant Physiol. 163:672-681(2013).
-!- FUNCTION: Involved in the catabolism of purine nucleotides. The
sequential activity of AAH, UGLYAH and UAH allows a complete
purine berakdown without the intermediate generation of urea.
{ECO:0000269|PubMed:23940254}.
-!- CATALYTIC ACTIVITY: Allantoate + H(2)O = (S)-ureidoglycine + NH(3)
+ CO(2). {ECO:0000269|PubMed:23940254}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=83 uM for allantoate {ECO:0000269|PubMed:23940254};
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AP003628; BAD45389.1; -; Genomic_DNA.
EMBL; AP008212; BAF20218.1; -; Genomic_DNA.
EMBL; AP014962; BAS99030.1; -; Genomic_DNA.
EMBL; CM000143; EEE66180.1; -; Genomic_DNA.
EMBL; AK073262; BAG93368.1; -; mRNA.
RefSeq; XP_015644100.1; XM_015788614.1.
UniGene; Os.11403; -.
ProteinModelPortal; Q655X8; -.
SMR; Q655X8; -.
STRING; 39947.LOC_Os06g45480.1; -.
PaxDb; Q655X8; -.
PRIDE; Q655X8; -.
EnsemblPlants; OS06T0665500-01; OS06T0665500-01; OS06G0665500.
GeneID; 4341777; -.
Gramene; OS06T0665500-01; OS06T0665500-01; OS06G0665500.
KEGG; osa:4341777; -.
eggNOG; ENOG410II0M; Eukaryota.
eggNOG; COG0624; LUCA.
HOGENOM; HOG000241291; -.
InParanoid; Q655X8; -.
KO; K02083; -.
OMA; CDEEGTR; -.
OrthoDB; EOG093608AX; -.
Proteomes; UP000059680; Chromosome 6.
Genevisible; Q655X8; OS.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0047652; F:allantoate deiminase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
GO; GO:0000256; P:allantoin catabolic process; TAS:UniProtKB.
GO; GO:0006145; P:purine nucleobase catabolic process; IEA:EnsemblPlants.
GO; GO:0010136; P:ureide catabolic process; IEA:EnsemblPlants.
CDD; cd03884; M20_bAS; 1.
InterPro; IPR010158; Amidase_Cbmase.
InterPro; IPR001261; ArgE/DapE_CS.
InterPro; IPR002933; Peptidase_M20.
InterPro; IPR011650; Peptidase_M20_dimer.
Pfam; PF07687; M20_dimer; 1.
Pfam; PF01546; Peptidase_M20; 1.
SUPFAM; SSF55031; SSF55031; 1.
TIGRFAMs; TIGR01879; hydantase; 1.
PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Hydrolase; Manganese;
Metal-binding; Purine metabolism; Reference proteome; Signal.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 491 Probable allantoate deiminase.
/FTId=PRO_0000423443.
COMPBIAS 385 388 Poly-Ala.
COMPBIAS 483 489 Poly-Ala.
METAL 122 122 Manganese 1. {ECO:0000250}.
METAL 131 131 Manganese 1. {ECO:0000250}.
METAL 131 131 Manganese 2. {ECO:0000250}.
METAL 168 168 Manganese 2. {ECO:0000250}.
METAL 234 234 Manganese 1. {ECO:0000250}.
METAL 454 454 Manganese 2. {ECO:0000250}.
CONFLICT 414 415 VR -> FP (in Ref. 4; EEE66180).
{ECO:0000305}.
SEQUENCE 491 AA; 52716 MW; 7F631B0C1FBEE731 CRC64;
MALLLSYPRR HPSIHLLILS AYALFLLPIL DGLELGGDGL YREILRDETV LRLKELGKIS
DGEGYLERTF LSPASIRASA VIISWMKDAG LTTWIDQMGN IHGRFEPTNS TKEALLIGSH
MDTVIDAGMY DGALGIISAI SALKVLKVTG RLQRLTRPVE VIAFSDEEGV RFQTTFLGSA
AVAGTLPESI LQVSDKSGTT VQDVLKLNSL EGTANALGEV RYSPESVGSY VEVHIEQGPV
LEALRYPLGV VKGIAGQTRL KVIINGSQGH AGTVPMKLRR DPMVAAAELV LTLETLCKEP
NKFLTYDEEC GCFTEESLAG LVCTVGELLT WPSASNVIPG QVNFTVDIRA MDDKVRETIV
TSFSRLVLQR CDDRLVDCAV EQKHAAAATP CDAELTSRLE RATRSTISSM AAGVRRAGGE
TPVLMSGAGH DAMAMARLTK VGMLFVRCRG GVSHSPEESV MDDDVWAAGL ALVNFIDQNA
VDAAAATAAE S


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