(data stored in SCRATCH zone)

SWISSPROT: D1CDR0_THET1

ID   D1CDR0_THET1            Unreviewed;       198 AA.
AC   D1CDR0;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Phosphoheptose isomerase {ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS00846111};
DE            EC=5.3.1.28 {ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS00846105};
DE   AltName: Full=Sedoheptulose 7-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00067};
GN   Name=gmhA {ECO:0000256|HAMAP-Rule:MF_00067};
GN   OrderedLocusNames=Tter_0144 {ECO:0000313|EMBL:ACZ41066.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41066.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41066.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate
CC       in D-glycero-D-manno-heptose 7-phosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_00067, ECO:0000256|SAAS:SAAS00846114}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-
CC         heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-
CC         phosphate; Xref=Rhea:RHEA:27489, ChEBI:CHEBI:57483,
CC         ChEBI:CHEBI:60203, ChEBI:CHEBI:60204; EC=5.3.1.28;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00067,
CC         ECO:0000256|SAAS:SAAS01116330};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00067};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00067};
CC   -!- PATHWAY: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-
CC       phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-
CC       phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from
CC       sedoheptulose 7-phosphate: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_00067, ECO:0000256|SAAS:SAAS00846100}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00067,
CC       ECO:0000256|SAAS:SAAS00846118}.
CC   -!- MISCELLANEOUS: The reaction produces a racemic mixture of D-
CC       glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-
CC       manno-heptose 7-phosphate. {ECO:0000256|HAMAP-Rule:MF_00067}.
CC   -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS00846117}.
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DR   EMBL; CP001825; ACZ41066.1; -; Genomic_DNA.
DR   RefSeq; WP_012874101.1; NC_013525.1.
DR   STRING; 525904.Tter_0144; -.
DR   EnsemblBacteria; ACZ41066; ACZ41066; Tter_0144.
DR   KEGG; ttr:Tter_0144; -.
DR   eggNOG; ENOG4105F55; Bacteria.
DR   eggNOG; COG0279; LUCA.
DR   HOGENOM; HOG000237571; -.
DR   KO; K03271; -.
DR   OMA; DVHICVP; -.
DR   OrthoDB; 1571626at2; -.
DR   BioCyc; TTER525904:G1GGS-146-MONOMER; -.
DR   UniPathway; UPA00041; UER00436.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0008968; F:D-sedoheptulose 7-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:2001061; P:D-glycero-D-manno-heptose 7-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05006; SIS_GmhA; 1.
DR   HAMAP; MF_00067; GmhA; 1.
DR   InterPro; IPR035461; GmhA/DiaA.
DR   InterPro; IPR004515; Phosphoheptose_Isoase.
DR   InterPro; IPR001347; SIS.
DR   Pfam; PF13580; SIS_2; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CDR0.
DR   SWISS-2DPAGE; D1CDR0.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00067,
KW   ECO:0000256|SAAS:SAAS00846094}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00067,
KW   ECO:0000256|SAAS:SAAS00846120};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00067,
KW   ECO:0000256|SAAS:SAAS00846084, ECO:0000313|EMBL:ACZ41066.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00067,
KW   ECO:0000256|SAAS:SAAS00846086};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS00846090}.
FT   DOMAIN       37    192       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   REGION       52     54       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00067}.
FT   REGION       94     95       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00067}.
FT   REGION      120    122       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00067}.
FT   COILED        6     26       {ECO:0000256|SAM:Coils}.
FT   METAL        61     61       Zinc. {ECO:0000256|HAMAP-Rule:MF_00067}.
FT   METAL        65     65       Zinc. {ECO:0000256|HAMAP-Rule:MF_00067}.
FT   METAL       172    172       Zinc. {ECO:0000256|HAMAP-Rule:MF_00067}.
FT   METAL       180    180       Zinc. {ECO:0000256|HAMAP-Rule:MF_00067}.
FT   BINDING      65     65       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00067}.
FT   BINDING     125    125       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00067}.
FT   BINDING     172    172       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00067}.
SQ   SEQUENCE   198 AA;  21357 MW;  1329A415430EBCB7 CRC64;
     MTISINNLLQ KRQEKLNVAI NQLIRDSELL ESVANTLIQS LCSNKKILIC GNGGSAAQAQ
     HMAGELIGRF KKNRAPIAAL ALGTDMATTT AIANDFGYEE VFLRQVDALG NDGDVLLILS
     TSGNSPNVLA AVNTARRKGL KTVAFTGKKP SKVEDLADIV VRFPAEETDV IQELHLLAIH
     ILCEVVEEHL SKEVVDGQ
//

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