(data stored in ACNUC7421 zone)

SWISSPROT: 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   05-JUL-2017, entry version 95.
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and 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
CC       enzyme in nitrogen utilization via the assimilation of allantoin.
CC       It is able to utilize allantoin as a sole source of nitrogen under
CC       anaerobic conditions. Catalyzes the oxidation of ureidoglycolate
CC       to oxalurate. {ECO:0000250|UniProtKB:P77555}.
CC   -!- CATALYTIC ACTIVITY: (S)-ureidoglycolate + NAD(+) = N-carbamoyl-2-
CC       oxoglycine + NADH. {ECO:0000250|UniProtKB:P77555}.
CC   -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation; oxalurate
CC       from (S)-ureidoglycolate: step 1/1.
CC       {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}.
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_MWVM01000032.1.
DR   ProteinModelPortal; P58408; -.
DR   SMR; P58408; -.
DR   STRING; 155864.Z0672; -.
DR   EnsemblBacteria; AAG54874; AAG54874; Z0672.
DR   EnsemblBacteria; BAB34002; BAB34002; BAB34002.
DR   GeneID; 916572; -.
DR   KEGG; ece:Z0672; -.
DR   KEGG; ecs:ECs0579; -.
DR   PATRIC; fig|386585.9.peg.686; -.
DR   eggNOG; ENOG4105DG4; Bacteria.
DR   eggNOG; COG2055; LUCA.
DR   HOGENOM; HOG000173270; -.
DR   KO; K00073; -.
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   InterPro; IPR003767; Malate/L-lactate_DH-like.
DR   InterPro; IPR017590; Ureidoglycolate_dehydrogenase.
DR   PANTHER; PTHR11091; PTHR11091; 1.
DR   PANTHER; PTHR11091:SF4; PTHR11091:SF4; 1.
DR   Pfam; PF02615; Ldh_2; 1.
DR   SUPFAM; SSF89733; SSF89733; 1.
DR   TIGRFAMs; TIGR03175; AllD; 1.
PE   3: Inferred from homology;
DR   PRODOM; P58408.
DR   SWISS-2DPAGE; P58408.
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase; Purine metabolism.
FT   CHAIN         1    349       Ureidoglycolate dehydrogenase (NAD(+)).
FT                                /FTId=PRO_0000083823.
FT   NP_BIND     174    176       NAD. {ECO:0000250|UniProtKB:P77555}.
FT   NP_BIND     306    308       NAD. {ECO:0000250|UniProtKB:P77555}.
FT   ACT_SITE    116    116       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:P77555}.
FT   BINDING     140    140       NAD. {ECO:0000250|UniProtKB:P77555}.
FT   BINDING     224    224       NAD. {ECO:0000250|UniProtKB:P77555}.
FT   SITE         48     48       Plays a crucial role in stabilizing the
FT                                binding of (S)-ureidoglycolate.
FT                                {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
//

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