ALLD_ECO57
ID ALLD_ECO57 Reviewed; 349 AA.
AC P58408;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Ureidoglycolate dehydrogenase (NAD(+)) {ECO:0000250|UniProtKB:P77555};
DE EC=1.1.1.350 {ECO:0000250|UniProtKB:P77555};
GN Name=allD {ECO:0000250|UniProtKB:P77555}; Synonyms=glxB8;
GN OrderedLocusNames=Z0672, ECs0579;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: AllD plays a pivotal role as a metabolic branch-point enzyme
CC in nitrogen utilization via the assimilation of allantoin. It is able
CC to utilize allantoin as a sole source of nitrogen under anaerobic
CC conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate.
CC {ECO:0000250|UniProtKB:P77555}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-ureidoglycolate + NAD(+) = H(+) + N-carbamoyl-2-oxoglycine
CC + NADH; Xref=Rhea:RHEA:15329, ChEBI:CHEBI:15378, ChEBI:CHEBI:57296,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57824, ChEBI:CHEBI:57945;
CC EC=1.1.1.350; Evidence={ECO:0000250|UniProtKB:P77555};
CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation; oxalurate from
CC (S)-ureidoglycolate: step 1/1. {ECO:0000250|UniProtKB:P77555}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P77555}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P77555}.
CC -!- INDUCTION: By glyoxylate and allantoin under anaerobic conditions.
CC {ECO:0000250|UniProtKB:P77555}.
CC -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.
CC {ECO:0000250|UniProtKB:P77555}.
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DR EMBL; AE005174; AAG54874.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34002.1; -; Genomic_DNA.
DR PIR; C90701; C90701.
DR PIR; F85551; F85551.
DR RefSeq; NP_308606.1; NC_002695.1.
DR RefSeq; WP_000703914.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P58408; -.
DR SMR; P58408; -.
DR STRING; 155864.EDL933_0602; -.
DR EnsemblBacteria; AAG54874; AAG54874; Z0672.
DR EnsemblBacteria; BAB34002; BAB34002; ECs_0579.
DR GeneID; 916572; -.
DR KEGG; ece:Z0672; -.
DR KEGG; ecs:ECs_0579; -.
DR PATRIC; fig|386585.9.peg.686; -.
DR eggNOG; COG2055; Bacteria.
DR HOGENOM; CLU_040452_3_1_6; -.
DR OMA; CSDYRGH; -.
DR UniPathway; UPA00395; UER00657.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0000256; P:allantoin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1530.10; -; 1.
DR Gene3D; 3.30.1370.60; -; 1.
DR InterPro; IPR043144; Mal/L-sulf/L-lact_DH-like_ah.
DR InterPro; IPR043143; Mal/L-sulf/L-lact_DH-like_NADP.
DR InterPro; IPR036111; Mal/L-sulfo/L-lacto_DH-like_sf.
DR InterPro; IPR003767; Malate/L-lactate_DH-like.
DR InterPro; IPR017590; Ureidoglycolate_dehydrogenase.
DR PANTHER; PTHR11091; PTHR11091; 1.
DR Pfam; PF02615; Ldh_2; 1.
DR SUPFAM; SSF89733; SSF89733; 1.
DR TIGRFAMs; TIGR03175; AllD; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Oxidoreductase; Purine metabolism; Reference proteome.
FT CHAIN 1..349
FT /note="Ureidoglycolate dehydrogenase (NAD(+))"
FT /id="PRO_0000083823"
FT ACT_SITE 116
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P77555"
FT BINDING 140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P77555"
FT BINDING 174..176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P77555"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P77555"
FT BINDING 306..308
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P77555"
FT SITE 48
FT /note="Plays a crucial role in stabilizing the binding of
FT (S)-ureidoglycolate"
FT /evidence="ECO:0000250|UniProtKB:P77555"
SQ SEQUENCE 349 AA; 37891 MW; 27E9E09DBD10C964 CRC64;
MKISRETLHQ LIENKLCQAG LKREHAATVA EVLVYADARG IHSHGAVRVE YYAERISKGG
TNREPEFRLE ETGPCSAILH ADNAAGQVAA KMGMEHAIKT AQQNGVAVVG ISRMGHSGAI
SYFVQQAARA GLIGISMCQS DPMVVPFGGA EIYYGTNPLA FAAPGEGDEI LTFDMATTVQ
AWGKVLDARS RNMSIPDTWA VDKNGAPTTD PFAVHALLPA AGPKGYGLMM MIDVLSGVLL
GLPFGRQVSS MYDDLHAGRN LGQLHVVINP NFFSSSELFR QHLSQTMREL NAITPAPGFN
QVYYPGQDQD IKQRQAAVEG IEIVDDIYQY LISDALYNTS YETKNPFAQ
