ALLA_PSEPK
ID ALLA_PSEPK Reviewed; 167 AA.
AC P59285;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Ureidoglycolate lyase {ECO:0000255|HAMAP-Rule:MF_00616};
DE EC=4.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00616};
DE AltName: Full=Ureidoglycolatase {ECO:0000255|HAMAP-Rule:MF_00616};
GN Name=allA {ECO:0000255|HAMAP-Rule:MF_00616}; OrderedLocusNames=PP_4288;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND SUBUNIT.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of the putative ureidoglycolate hydrolase pp4288 from
RT Pseudomonas putida, Northeast structural genomics target Ppr49.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the catabolism of the allantoin degradation
CC intermediate (S)-ureidoglycolate, generating urea and glyoxylate.
CC Involved in the utilization of allantoin as nitrogen source.
CC {ECO:0000255|HAMAP-Rule:MF_00616}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-ureidoglycolate = glyoxylate + urea; Xref=Rhea:RHEA:11304,
CC ChEBI:CHEBI:16199, ChEBI:CHEBI:36655, ChEBI:CHEBI:57296; EC=4.3.2.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00616};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00616};
CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation.
CC {ECO:0000255|HAMAP-Rule:MF_00616}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00616,
CC ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the ureidoglycolate lyase family.
CC {ECO:0000255|HAMAP-Rule:MF_00616}.
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DR EMBL; AE015451; AAN69868.1; -; Genomic_DNA.
DR RefSeq; NP_746404.1; NC_002947.4.
DR RefSeq; WP_003254333.1; NC_002947.4.
DR PDB; 2BDR; X-ray; 1.60 A; A/B=1-167.
DR PDBsum; 2BDR; -.
DR AlphaFoldDB; P59285; -.
DR SMR; P59285; -.
DR STRING; 160488.PP_4288; -.
DR EnsemblBacteria; AAN69868; AAN69868; PP_4288.
DR KEGG; ppu:PP_4288; -.
DR PATRIC; fig|160488.4.peg.4560; -.
DR eggNOG; COG3194; Bacteria.
DR HOGENOM; CLU_070848_1_0_6; -.
DR OMA; WNIFRCS; -.
DR PhylomeDB; P59285; -.
DR BioCyc; PPUT160488:G1G01-4566-MON; -.
DR UniPathway; UPA00395; -.
DR EvolutionaryTrace; P59285; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0004848; F:ureidoglycolate hydrolase activity; IEA:InterPro.
DR GO; GO:0050385; F:ureidoglycolate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000256; P:allantoin catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.120.480; -; 1.
DR HAMAP; MF_00616; Ureidogly_lyase; 1.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR007247; Ureidogly_lyase.
DR InterPro; IPR023525; Ureidogly_lyase_bac.
DR InterPro; IPR024060; Ureidoglycolate_lyase_dom_sf.
DR PANTHER; PTHR21221; PTHR21221; 1.
DR Pfam; PF04115; Ureidogly_lyase; 1.
DR PIRSF; PIRSF017306; Ureidogly_hydro; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Purine metabolism; Reference proteome.
FT CHAIN 1..167
FT /note="Ureidoglycolate lyase"
FT /id="PRO_0000120551"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:2BDR"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:2BDR"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2BDR"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2BDR"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 130..144
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:2BDR"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2BDR"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2BDR"
SQ SEQUENCE 167 AA; 18768 MW; 670B9A0AF8A8B1D3 CRC64;
MRTLMIEPLT KEAFAQFGDV IETDGSDHFM INNGSTMRFH KLATVETAEP EDKAIISIFR
ADAQDMPLTV RMLERHPLGS QAFIPLLGNP FLIVVAPVGD APVSGLVRAF RSNGRQGVNY
HRGVWHHPVL TIEKRDDFLV VDRSGSGNNC DEHYFTEEQM LILNPHQ
