ID   HLDD_CHRSD              Reviewed;         318 AA.
AC   Q1R1N5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   16-JUN-2009, entry version 25.
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=Csal_0008;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000285; ABE57373.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_572072.1; -.
DR   GeneID; 4027327; -.
DR   GenomeReviews; CP000285_GR; Csal_0008.
DR   KEGG; csa:Csal_0008; -.
DR   NMPDR; fig|290398.4.peg.150; -.
DR   HOGENOM; Q1R1N5; -.
DR   BioCyc; CSAL290398:CSAL_0008-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   Carbohydrate metabolism; Complete proteome; Isomerase; NADP.
FT   CHAIN         1    318       ADP-L-glycero-D-manno-heptose-6-
FT                                epimerase.
FT                                /FTId=PRO_0000255726.
FT   NP_BIND      10     11       NADP (By similarity).
FT   NP_BIND      31     32       NADP (By similarity).
FT   NP_BIND      80     84       NADP (By similarity).
FT   REGION      205    208       Substrate binding (By similarity).
FT   ACT_SITE    144    144       Proton acceptor (By similarity).
FT   ACT_SITE    182    182       Proton acceptor (By similarity).
FT   BINDING      38     38       NADP (By similarity).
FT   BINDING      53     53       NADP (By similarity).
FT   BINDING      97     97       NADP (By similarity).
FT   BINDING     148    148       NADP (By similarity).
FT   BINDING     173    173       Substrate (By similarity).
FT   BINDING     174    174       NADP; via amide nitrogen (By similarity).
FT   BINDING     182    182       NADP (By similarity).
FT   BINDING     184    184       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     191    191       Substrate (By similarity).
FT   BINDING     218    218       Substrate (By similarity).
FT   BINDING     282    282       Substrate (By similarity).
SQ   SEQUENCE   318 AA;  35939 MW;  D87EC102A8046625 CRC64;
     MIVVTGGAGF IGANLVKALN ARGREDVLVV DDLSDGTKFV NLADCTLGDY LDKDDFLARV
     KAELRGEPSE LPPIEAIFHE GACSDTTEWD GKFMLENNFE YSKVLLHFCQ YKRIPFLYAS
     SAATYGGSEV FVEAPEHEKP LNVYGYSKLL FDQYVRVHWE SFDAQVVGFR YFNVYGPREQ
     HKGKMASVAY HHHSQVKRGE NPKLFGAWDG YEAGMQSRDF VYVGDVVDVN LWCLDHPEVS
     GIFNLGTGRA EPFKAIAETV IDYYATGKID YIDFPEELKG RYQSYTRADI SRLREAGYKA
     EFKTVREGVS AYLDWLNG
//