AAH2_SOYBN
ID AAH2_SOYBN Reviewed; 483 AA.
AC I1L153;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Allantoate deiminase 2 {ECO:0000305};
DE EC=3.5.3.9 {ECO:0000269|PubMed:23940254};
DE AltName: Full=Allantoate amidohydrolase 2 {ECO:0000303|PubMed:23940254};
DE Short=GmAAH2 {ECO:0000303|PubMed:23940254};
DE Flags: Precursor;
GN Name=AAH2 {ECO:0000303|PubMed:23940254}; OrderedLocusNames=Glyma09g05600;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000312|Proteomes:UP000008827};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82; TISSUE=Callus;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=23940254; DOI=10.1104/pp.113.224261;
RA Werner A.K., Medina-Escobar N., Zulawski M., Sparkes I.A., Cao F.Q.,
RA Witte C.P.;
RT "The ureide-degrading reactions of purine ring catabolism employ three
RT amidohydrolases and one aminohydrolase in Arabidopsis, soybean, and rice.";
RL Plant Physiol. 163:672-681(2013).
CC -!- FUNCTION: Involved in the catabolism of purine nucleotides. Can use
CC allantoate as substrate. The sequential activity of AAH, UGLYAH and UAH
CC allows a complete purine breakdown without the intermediate generation
CC of urea. {ECO:0000269|PubMed:23940254}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allantoate + 2 H(+) + H2O = (S)-2-ureidoglycine + CO2 +
CC NH4(+); Xref=Rhea:RHEA:27485, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:17536, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:59947; EC=3.5.3.9;
CC Evidence={ECO:0000269|PubMed:23940254};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:C0M0V4};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=102 uM for allantoate {ECO:0000269|PubMed:23940254};
CC Note=kcat is 34 sec(-1) for allantoate.
CC {ECO:0000269|PubMed:23940254};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:C0M0V4}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:C0M0V4}.
CC -!- TISSUE SPECIFICITY: Expressed in stems and leaves, and at low levels in
CC roots. Not detected in nodules. {ECO:0000269|PubMed:23940254}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; CM000842; KRH37194.1; -; Genomic_DNA.
DR RefSeq; XP_003533667.1; XM_003533619.3.
DR AlphaFoldDB; I1L153; -.
DR SMR; I1L153; -.
DR STRING; 3847.GLYMA09G05600.1; -.
DR MEROPS; M20.A07; -.
DR PRIDE; I1L153; -.
DR EnsemblPlants; KRH37194; KRH37194; GLYMA_09G050800.
DR Gramene; KRH37194; KRH37194; GLYMA_09G050800.
DR eggNOG; ENOG502QSJ5; Eukaryota.
DR HOGENOM; CLU_024588_6_1_1; -.
DR InParanoid; I1L153; -.
DR OrthoDB; 529725at2759; -.
DR SABIO-RK; I1L153; -.
DR Proteomes; UP000008827; Chromosome 9.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0047652; F:allantoate deiminase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR32494; PTHR32494; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01879; hydantase; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Manganese; Metal-binding;
KW Purine metabolism; Reference proteome; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..483
FT /note="Allantoate deiminase 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5009336373"
FT BINDING 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9D1A2"
FT BINDING 136
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9D1A2"
FT BINDING 136
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9D1A2"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9D1A2"
FT BINDING 239
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9D1A2"
FT BINDING 457
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9D1A2"
SQ SEQUENCE 483 AA; 52353 MW; 7E9521B1AF259A49 CRC64;
MSSATASNTF FLHSCFLLFC LLSAPSCVSM FSGIETGDLE KRDDLFPQIL RDEAVARLYE
LGKVSDASGY LERTFLSPAS MRAINLIRKW MEDAGLRTWV DQMGNVHGRV DGANANAEAL
LIGSHMDTVV DAGMFDGSLG IVSAISALKA MHVNGKLQKL KRPVEVIAFS DEEGVRFQTT
FLGSGAIAGI LPGTTLEISD KREVMIKDFL KENSIDITEE SLLKLKYDPK SVWGYVEVHI
EQGPVLEQVG FPLGVVKGIA GQTRLKVTVR GSQGHAGTVP MSMRQDPMAA AAEQIVVLES
LCKHPEEYLS YDGHCSDSTV KSLSTSLVCT VGEISTWPSA SNVIPGQVTY TVDIRAIDDL
GREAVIYDLS KQIYQICDKR SVSCIIEHKH DAGAVICDSD LSSQLKSAAY SALKKMEGDI
QDEVPTLMSG AGHDAMAISH LTKVGMLFVR CRGGISHSPQ EHVLDNDVWA ASLATLSFLE
NLS
