ALLA_PSEF5
ID ALLA_PSEF5 Reviewed; 167 AA.
AC Q4K8H2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=PFL_4369;
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
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 -!- SIMILARITY: Belongs to the ureidoglycolate lyase family.
CC {ECO:0000255|HAMAP-Rule:MF_00616}.
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DR EMBL; CP000076; AAY93624.1; -; Genomic_DNA.
DR RefSeq; WP_011062639.1; NC_004129.6.
DR AlphaFoldDB; Q4K8H2; -.
DR SMR; Q4K8H2; -.
DR STRING; 220664.PFL_4369; -.
DR EnsemblBacteria; AAY93624; AAY93624; PFL_4369.
DR GeneID; 57477446; -.
DR KEGG; pfl:PFL_4369; -.
DR PATRIC; fig|220664.5.peg.4476; -.
DR eggNOG; COG3194; Bacteria.
DR HOGENOM; CLU_070848_1_0_6; -.
DR OMA; WNIFRCS; -.
DR OrthoDB; 1597997at2; -.
DR UniPathway; UPA00395; -.
DR Proteomes; UP000008540; 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 3: Inferred from homology;
KW Lyase; Purine metabolism; Reference proteome.
FT CHAIN 1..167
FT /note="Ureidoglycolate lyase"
FT /id="PRO_1000061362"
SQ SEQUENCE 167 AA; 18740 MW; 1B100573199EB14E CRC64;
MRTLVIEPLS KEAFAPFGDV IETDGSDHFM INNGSTMRFH RLATVETAQP EDQAIISIFR
ADALDMPLTI RMLERHPLGS QAFIPLLGNP FLIVVAPLGD EPVSGLVRAF VSNGRQGINY
HRGVWHHPVL TIEKRDDFLV VDRSGTGNNC DEHFFKEDER LILAPHQ