ID   HLDD_ECOL5              Reviewed;         310 AA.
AC   Q0TBI8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=ADP-L-glycero-D-manno-heptose-6-epimerase;
DE            EC=5.1.3.20;
DE   AltName: Full=ADP-L-glycero-beta-D-manno-heptose-6-epimerase;
DE            Short=ADP-glyceromanno-heptose 6-epimerase;
DE            Short=ADP-hep 6-epimerase;
DE            Short=AGME;
GN   Name=hldD; OrderedLocusNames=ECP_3719;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
CC   -!- FUNCTION: Catalyzes the interconversion between ADP-D-glycero-
CC       beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an
CC       epimerization at carbon 6 of the heptose (By similarity).
CC   -!- CATALYTIC ACTIVITY: ADP-D-glycero-D-manno-heptose = ADP-L-glycero-
CC       D-manno-heptose.
CC   -!- COFACTOR: Binds 1 NADP(+) per subunit (By similarity).
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-
CC       manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose
CC       from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4.
CC   -!- SUBUNIT: Homopentamer (By similarity).
CC   -!- DOMAIN: Contains a large N-terminal NADP-binding domain, and a
CC       smaller C-terminal substrate-binding domain (By similarity).
CC   -!- SIMILARITY: Belongs to the sugar epimerase family. HldD subfamily.
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DR   EMBL; CP000247; ABG71691.1; -; Genomic_DNA.
DR   RefSeq; YP_671592.1; -.
DR   SMR; Q0TBI8; 1-307.
DR   GeneID; 4190289; -.
DR   GenomeReviews; CP000247_GR; ECP_3719.
DR   KEGG; ecp:ECP_3719; -.
DR   HOGENOM; Q0TBI8; -.
DR   OMA; Q0TBI8; FGPNEYH.
DR   BioCyc; ECOL362663:ECP_3719-MON; -.
DR   GO; GO:0008712; F:ADP-glyceromanno-heptose 6-epimerase activity; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:HAMAP.
DR   GO; GO:0044237; P:cellular metabolic process; IEA:InterPro.
DR   HAMAP; MF_01601; -; 1.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR011912; Heptose_epim.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR10366:SF29; Heptose_epim; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   TIGRFAMs; TIGR02197; heptose_epim; 1.
PE   3: Inferred from homology;
KW   Acetylation; Carbohydrate metabolism; Complete proteome; Isomerase;
KW   NADP.
FT   CHAIN         1    310       ADP-L-glycero-D-manno-heptose-6-
FT                                epimerase.
FT                                /FTId=PRO_0000255730.
FT   NP_BIND      10     11       NADP (By similarity).
FT   NP_BIND      31     32       NADP (By similarity).
FT   NP_BIND      75     79       NADP (By similarity).
FT   REGION      201    204       Substrate binding (By similarity).
FT   ACT_SITE    140    140       Proton acceptor (By similarity).
FT   ACT_SITE    178    178       Proton acceptor (By similarity).
FT   BINDING      38     38       NADP (By similarity).
FT   BINDING      53     53       NADP (By similarity).
FT   BINDING      92     92       NADP (By similarity).
FT   BINDING     144    144       NADP (By similarity).
FT   BINDING     169    169       Substrate (By similarity).
FT   BINDING     170    170       NADP; via amide nitrogen (By similarity).
FT   BINDING     178    178       NADP (By similarity).
FT   BINDING     180    180       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     187    187       Substrate (By similarity).
FT   BINDING     209    209       Substrate (By similarity).
FT   BINDING     272    272       Substrate (By similarity).
FT   MOD_RES     267    267       N6-acetyllysine (By similarity).
SQ   SEQUENCE   310 AA;  34894 MW;  499122A87C041522 CRC64;
     MIIVTGGAGF IGSNIVKALN DKGITDILVV DNLKDGTKFV NLVDLDIADY MDKEDFLIQI
     MAGEEFGDVE AIFHEGACSS TTEWDGKYMM DNNYQYSKEL LHYCLEREIP FLYASSAATY
     GGRTSDFIES REYEKPLNVY GYSKFLFDEY VRQILPEANS QIVGFRYFNV YGPREGHKGS
     MASVAFHLNT QLNNGESPKL FEGSENFKRD FVYVGDVADV NLWFLENGVS GIFNLGTGRA
     ESFQAVADAT LAYHKKGQIE YIPFPDKLKG RYQAFTQADL TNLRAAGYDK PFKTVAEGVT
     EYMAWLNRDA
//