ALLC_CHLRE
ID ALLC_CHLRE Reviewed; 162 AA.
AC P82678; A0A2K3D8W0; A2PZB4;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Allantoicase {ECO:0000303|PubMed:10860551};
DE EC=3.5.3.4 {ECO:0000269|PubMed:10860551};
DE AltName: Full=Allantoate amidinohydrolase {ECO:0000303|PubMed:10860551};
DE AltName: Full=Protein EARLY ZYGOTE EXPRESSED 3 {ECO:0000303|PubMed:18487630};
GN Name=EZY3 {ECO:0000303|PubMed:18487630};
GN ORFNames=CHLRE_11g482650v5 {ECO:0000312|EMBL:PNW76956.1},
GN CHLREDRAFT_192916 {ECO:0000312|EMBL:EDP00347.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=18487630; DOI=10.1093/pcp/pcn076;
RA Kubo T., Abe J., Oyamada T., Ohnishi M., Fukuzawa H., Matsuda Y., Saito T.;
RT "Characterization of novel genes induced by sexual adhesion and gamete
RT fusion and of their transcriptional regulation in Chlamydomonas
RT reinhardtii.";
RL Plant Cell Physiol. 49:981-993(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [3]
RP PROTEIN SEQUENCE OF 80-88, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RC STRAIN=6145C;
RX PubMed=10860551; DOI=10.1006/abbi.2000.1833;
RA Piedras P., Munoz A., Aguilar M., Pineda M.;
RT "Allantoate amidinohydrolase (Allantoicase) from Chlamydomonas reinhardtii:
RT its purification and catalytic and molecular characterization.";
RL Arch. Biochem. Biophys. 378:340-348(2000).
CC -!- FUNCTION: Catalyzes the degradation of allantoate to (-)-
CC ureidoglycolate and (+)-ureidoglycolate to glyoxylate.
CC {ECO:0000269|PubMed:10860551}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allantoate + H2O = (S)-ureidoglycolate + urea;
CC Xref=Rhea:RHEA:11016, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199,
CC ChEBI:CHEBI:17536, ChEBI:CHEBI:57296; EC=3.5.3.4;
CC Evidence={ECO:0000269|PubMed:10860551};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.0 mM for allantoate {ECO:0000269|PubMed:10860551};
CC KM=0.7 mM for ureidoglycolate {ECO:0000269|PubMed:10860551};
CC Note=Vmax of the reaction with allantoate as substrate is nine times
CC higher than that with ureidoglycolate. {ECO:0000269|PubMed:10860551};
CC pH dependence:
CC Optimum pH is 6.5 with allantoate as substrate, and 8 with
CC ureidoglycolate as substrate. {ECO:0000269|PubMed:10860551};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:10860551};
CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation; (S)-
CC ureidoglycolate from allantoate (aminidohydrolase route): step 1/1.
CC {ECO:0000269|PubMed:10860551}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:10860551}.
CC -!- TISSUE SPECIFICITY: Expressed in zygote. {ECO:0000269|PubMed:18487630}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the mating reaction and during early
CC zygote formation. {ECO:0000269|PubMed:18487630}.
CC -!- SIMILARITY: Belongs to the allantoicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=PNW76956.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB267730; BAF46276.1; -; mRNA.
DR EMBL; DS496140; EDP00347.1; -; Genomic_DNA.
DR EMBL; CM008972; PNW76956.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001697407.1; XM_001697355.1.
DR EnsemblPlants; PNW76956; PNW76956; CHLRE_11g482650v5.
DR GeneID; 5722959; -.
DR Gramene; PNW76956; PNW76956; CHLRE_11g482650v5.
DR HOGENOM; CLU_1637821_0_0_1; -.
DR OrthoDB; 1833733at2759; -.
DR BioCyc; MetaCyc:MON-13513; -.
DR SABIO-RK; P82678; -.
DR UniPathway; UPA00395; UER00654.
DR Proteomes; UP000006906; Chromosome 11.
DR GO; GO:0004037; F:allantoicase activity; IDA:UniProtKB.
DR GO; GO:0000256; P:allantoin catabolic process; IDA:UniProtKB.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Purine metabolism;
KW Reference proteome.
FT CHAIN 1..162
FT /note="Allantoicase"
FT /id="PRO_0000205915"
FT CONFLICT 84
FT /note="P -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="G -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 162 AA; 17207 MW; 10F498D097303466 CRC64;
MASTSHNPFY AAMQPQAQHW GATSPTSTGA GYDRPSAGYP AYTGYAAAGT SHPAPSSSSP
STALALYNPS SLYGLYYNEA VHGPFATGLQ SNPFTPGLAP LSTVSRPSYA TEDPLRQRYP
ATSANPHDPL NWITEDLFAI RMERAAISQQ RTPLRSASVA AR
