ALLE_ECOLI
ID ALLE_ECOLI Reviewed; 261 AA.
AC P75713; O54410; P77128; Q2MBR3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=(S)-ureidoglycine aminohydrolase {ECO:0000303|PubMed:20038185};
DE Short=UGHY {ECO:0000303|PubMed:20038185};
DE Short=UGlyAH;
DE EC=3.5.3.26 {ECO:0000269|PubMed:19935661, ECO:0000305|PubMed:20038185};
GN Name=allE; Synonyms=glxB6, ylbA; OrderedLocusNames=b0515, JW0503;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=K12 / ECL1;
RX PubMed=10601204; DOI=10.1128/jb.181.24.7479-7484.1999;
RA Cusa E., Obradors N., Baldoma L., Badia J., Aguilar J.;
RT "Genetic analysis of a chromosomal region containing genes required for
RT assimilation of allantoin nitrogen and linked glyoxylate metabolism in
RT Escherichia coli.";
RL J. Bacteriol. 181:7479-7484(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=20038185; DOI=10.1021/cb900248n;
RA Serventi F., Ramazzina I., Lamberto I., Puggioni V., Gatti R.,
RA Percudani R.;
RT "Chemical basis of nitrogen recovery through the ureide pathway: formation
RT and hydrolysis of S-ureidoglycine in plants and bacteria.";
RL ACS Chem. Biol. 5:203-214(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=19935661; DOI=10.1038/nchembio.265;
RA Werner A.K., Romeis T., Witte C.P.;
RT "Ureide catabolism in Arabidopsis thaliana and Escherichia coli.";
RL Nat. Chem. Biol. 6:19-21(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-261, AND SUBUNIT.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of ylbA, hypothetical protein from E.coli.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: Involved in the anaerobic nitrogen utilization via the
CC assimilation of allantoin. Catalyzes the second stereospecific
CC hydrolysis reaction (deamination) of the allantoin degradation pathway,
CC producing S-ureidoglycolate and ammonia from S-ureidoglycine.
CC {ECO:0000269|PubMed:19935661, ECO:0000269|PubMed:20038185}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2-ureidoglycine + H2O = (S)-ureidoglycolate + NH4(+);
CC Xref=Rhea:RHEA:25241, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57296, ChEBI:CHEBI:59947; EC=3.5.3.26;
CC Evidence={ECO:0000269|PubMed:19935661, ECO:0000305|PubMed:20038185};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20038185};
CC Note=Also able to use Co(2+)). {ECO:0000269|PubMed:20038185};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:20038185, ECO:0000305|Ref.7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19935661,
CC ECO:0000269|PubMed:20038185}.
CC -!- INDUCTION: By glyoxylate and allantoin under anaerobic conditions.
CC {ECO:0000305|PubMed:10601204}.
CC -!- SIMILARITY: Belongs to the UGHY family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB93856.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U89279; AAB93856.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U82664; AAB40267.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73617.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76293.1; -; Genomic_DNA.
DR PIR; B64783; B64783.
DR RefSeq; NP_415048.1; NC_000913.3.
DR RefSeq; WP_000540997.1; NZ_SSZK01000024.1.
DR PDB; 1RC6; X-ray; 2.60 A; A/B=1-261.
DR PDBsum; 1RC6; -.
DR AlphaFoldDB; P75713; -.
DR SMR; P75713; -.
DR BioGRID; 4262016; 8.
DR DIP; DIP-12689N; -.
DR IntAct; P75713; 7.
DR STRING; 511145.b0515; -.
DR jPOST; P75713; -.
DR PaxDb; P75713; -.
DR PRIDE; P75713; -.
DR EnsemblBacteria; AAC73617; AAC73617; b0515.
DR EnsemblBacteria; BAE76293; BAE76293; BAE76293.
DR GeneID; 945149; -.
DR KEGG; ecj:JW0503; -.
DR KEGG; eco:b0515; -.
DR PATRIC; fig|511145.12.peg.535; -.
DR EchoBASE; EB3387; -.
DR eggNOG; COG3257; Bacteria.
DR HOGENOM; CLU_056083_3_0_6; -.
DR InParanoid; P75713; -.
DR OMA; DVRHDMH; -.
DR PhylomeDB; P75713; -.
DR BioCyc; EcoCyc:G6284-MON; -.
DR BioCyc; MetaCyc:G6284-MON; -.
DR BRENDA; 3.5.3.26; 2026.
DR EvolutionaryTrace; P75713; -.
DR PRO; PR:P75713; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0071522; F:ureidoglycine aminohydrolase activity; IDA:EcoCyc.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR CDD; cd02212; cupin_UGlyAH_C; 1.
DR CDD; cd02211; cupin_UGlyAH_N; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR013096; Cupin_2.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR017627; UGHY.
DR InterPro; IPR044697; UGlyAH_cupin_C.
DR InterPro; IPR008579; UGlyAH_Cupin_dom.
DR InterPro; IPR044704; UGlyAH_cupin_N.
DR Pfam; PF07883; Cupin_2; 1.
DR Pfam; PF05899; Cupin_3; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR03214; ura-cupin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW Purine metabolism; Reference proteome.
FT CHAIN 1..261
FT /note="(S)-ureidoglycine aminohydrolase"
FT /id="PRO_0000168644"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT BINDING 198
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT BINDING 236
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT CONFLICT 204
FT /note="A -> T (in Ref. 1; AAB93856 and 2; AAB40267)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..261
FT /note="GDYIFMGAYSLQAGYGVGRGEAFSYIYSKDCNRDVEI -> RRLHLYGRLFF
FT TGWLWCRAW (in Ref. 2; AAB40267)"
FT /evidence="ECO:0000305"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1RC6"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:1RC6"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 58..74
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 81..96
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1RC6"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 202..217
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:1RC6"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:1RC6"
SQ SEQUENCE 261 AA; 28730 MW; B424C7DBD34508D6 CRC64;
MGYLNNVTGY REDLLANRAI VKHGNFALLT PDGLVKNIIP GFENCDATIL STPKLGASFV
DYLVTLHQNG GNQQGFGGEG IETFLYVISG NITAKAEGKT FALSEGGYLY CPPGSLMTFV
NAQAEDSQIF LYKRRYVPVE GYAPWLVSGN ASELERIHYE GMDDVILLDF LPKELGFDMN
MHILSFAPGA SHGYIETHVQ EHGAYILSGQ GVYNLDNNWI PVKKGDYIFM GAYSLQAGYG
VGRGEAFSYI YSKDCNRDVE I
