AAH1_SOYBN
ID AAH1_SOYBN Reviewed; 483 AA.
AC C0M0V4; A9GYV1; I1MGU4;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Allantoate deiminase 1 {ECO:0000305};
DE EC=3.5.3.9 {ECO:0000269|PubMed:18065556};
DE AltName: Full=Allantoate amidohydrolase 1 {ECO:0000303|PubMed:23940254};
DE Short=GmAAH1 {ECO:0000303|PubMed:23940254};
DE Flags: Precursor;
GN Name=AAH1 {ECO:0000303|PubMed:23940254}; OrderedLocusNames=Glyma15g16870;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Williams 82; TISSUE=Leaf;
RX PubMed=18065556; DOI=10.1104/pp.107.110809;
RA Werner A.K., Sparkes I.A., Romeis T., Witte C.P.;
RT "Identification, biochemical characterization, and subcellular localization
RT of allantoate amidohydrolases from Arabidopsis and soybean.";
RL Plant Physiol. 146:418-430(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INDUCTION BY DROUGHT.
RC STRAIN=cv. Williams 82;
RX PubMed=19129162; DOI=10.1093/jxb/ern332;
RA Charlson D.V., Korth K.L., Purcell L.C.;
RT "Allantoate amidohydrolase transcript expression is independent of drought
RT tolerance in soybean.";
RL J. Exp. Bot. 60:847-851(2009).
RN [3]
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 [4]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE 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:18065556, ECO:0000269|PubMed:19129162}.
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; Evidence={ECO:0000269|PubMed:18065556,
CC ECO:0000269|PubMed:23940254};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18065556};
CC -!- ACTIVITY REGULATION: Inhibited by borate, fluoride, L-Asn and L-Asp.
CC {ECO:0000269|PubMed:18065556}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=72 uM for allantoate {ECO:0000269|PubMed:23940254};
CC Note=kcat is 37 sec(-1) for allantoate.
CC {ECO:0000269|PubMed:23940254};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18065556}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:18065556}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=C0M0V4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=C0M0V4-2; Sequence=VSP_058827;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and leaves. Not detected
CC in nodules. {ECO:0000269|PubMed:23940254}.
CC -!- INDUCTION: Not regulated during water-deficit stress.
CC {ECO:0000269|PubMed:19129162}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; AM773229; CAO78893.1; -; mRNA.
DR EMBL; FJ796239; ACN87318.1; -; mRNA.
DR EMBL; CM000848; KRH12172.1; -; Genomic_DNA.
DR EMBL; CM000848; KRH12173.1; -; Genomic_DNA.
DR EMBL; CM000848; KRH12175.1; -; Genomic_DNA.
DR EMBL; CM000848; KRH12174.1; -; Genomic_DNA.
DR RefSeq; NP_001236563.1; NM_001249634.1. [C0M0V4-1]
DR RefSeq; XP_006596931.1; XM_006596868.2.
DR RefSeq; XP_014622795.1; XM_014767309.1. [C0M0V4-1]
DR RefSeq; XP_014622796.1; XM_014767310.1. [C0M0V4-1]
DR AlphaFoldDB; C0M0V4; -.
DR SMR; C0M0V4; -.
DR STRING; 3847.GLYMA15G16870.3; -.
DR MEROPS; M20.A07; -.
DR PRIDE; C0M0V4; -.
DR EnsemblPlants; KRH12172; KRH12172; GLYMA_15G156900. [C0M0V4-1]
DR EnsemblPlants; KRH12173; KRH12173; GLYMA_15G156900. [C0M0V4-1]
DR EnsemblPlants; KRH12174; KRH12174; GLYMA_15G156900. [C0M0V4-2]
DR EnsemblPlants; KRH12175; KRH12175; GLYMA_15G156900. [C0M0V4-2]
DR GeneID; 100137075; -.
DR Gramene; KRH12172; KRH12172; GLYMA_15G156900. [C0M0V4-1]
DR Gramene; KRH12173; KRH12173; GLYMA_15G156900. [C0M0V4-1]
DR Gramene; KRH12174; KRH12174; GLYMA_15G156900. [C0M0V4-2]
DR Gramene; KRH12175; KRH12175; GLYMA_15G156900. [C0M0V4-2]
DR KEGG; gmx:100137075; -.
DR eggNOG; ENOG502QSJ5; Eukaryota.
DR HOGENOM; CLU_024588_6_1_1; -.
DR InParanoid; C0M0V4; -.
DR OrthoDB; 529725at2759; -.
DR BRENDA; 3.5.3.9; 2483.
DR SABIO-RK; C0M0V4; -.
DR Proteomes; UP000008827; Chromosome 15.
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 Alternative splicing; Endoplasmic reticulum; Hydrolase; Manganese;
KW Metal-binding; Purine metabolism; Reference proteome; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..483
FT /note="Allantoate deiminase 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5009331204"
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"
FT VAR_SEQ 1..80
FT /note="Missing (in isoform 2)"
FT /id="VSP_058827"
FT CONFLICT 2
FT /note="Y -> S (in Ref. 1; CAO78893)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 52396 MW; 35D7B4D8E045CF2F CRC64;
MYSATASNTF FLLSCFLLFC LLSAPSCVSM FSGIETGDLE KRDDLFPQIL RDEAVARLYE
LGKVSDASGY LERTFLSPAS MKAIDLIRKW MEDAGLRTWV DQMGNVHGRV DGANENAEAL
LIGSHMDTVV DAGMFDGSLG IVSAISAVKA MHVNGKLQKL KRPVEVIAFS DEEGVRFQTT
FLGSGAIAGI LPGTTLEISD KREVMIKDFL KENSMDITEE SLLKLKYDPK SVWGYVEVHI
EQGPVLEQVG FPLGVVKGIA GQTRLKVTVR GSQGHAGTVP MSMRQDPMAA AAEQIVVLES
LCKHPEEYLS YDGHCSDSTV KSLSSSLVCT VGEISTWPSA SNVIPGQVTY TVDIRAIDDL
GREAVIYDLS KQIYQICDKR SVSCIIEHKH DAGAVICDSD LSSQLKSAAY SALKKMEGDI
QDEVPTLMSG AGHDAMAISH LTKVGMLFVR CRGGISHSPQ EHVLDNDVWA AGLATLSFLE
NLS
