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Database: UniProt
Entry: D3SLB9_THEAH
LinkDB: D3SLB9_THEAH
Original site: D3SLB9_THEAH 
ID   D3SLB9_THEAH            Unreviewed;       316 AA.
AC   D3SLB9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Bifunctional phosphoglucose/phosphomannose isomerase {ECO:0000313|EMBL:ADC89549.1};
DE            EC=5.3.1.8 {ECO:0000313|EMBL:ADC89549.1};
GN   OrderedLocusNames=Thal_0917 {ECO:0000313|EMBL:ADC89549.1};
OS   Thermocrinis albus (strain DSM 14484 / JCM 11386 / HI 11/12).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX   NCBI_TaxID=638303 {ECO:0000313|EMBL:ADC89549.1, ECO:0000313|Proteomes:UP000002043};
RN   [1] {ECO:0000313|Proteomes:UP000002043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14484 / JCM 11386 / HI 11/12
RC   {ECO:0000313|Proteomes:UP000002043};
RX   DOI=10.4056/sigs.761490;
RA   Wirth R., Sikorski J., Brambilla E., Misra M., Lapidus A., Copeland A.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Tapia R., Bruce D., Goodwin L., Pitluck S., Pati A., Anderson I.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA   Bilek Y., Hader T., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Thermocrinis albus type strain (HI 11/12T).";
RL   Stand. Genomic Sci. 2:194-202(2010).
CC   -!- SIMILARITY: Belongs to the PGI/PMI family.
CC       {ECO:0000256|ARBA:ARBA00010523}.
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DR   EMBL; CP001931; ADC89549.1; -; Genomic_DNA.
DR   RefSeq; WP_012991955.1; NC_013894.1.
DR   AlphaFoldDB; D3SLB9; -.
DR   STRING; 638303.Thal_0917; -.
DR   KEGG; tal:Thal_0917; -.
DR   eggNOG; COG2222; Bacteria.
DR   HOGENOM; CLU_059687_0_0_0; -.
DR   OMA; FPELNHN; -.
DR   OrthoDB; 9771734at2; -.
DR   Proteomes; UP000002043; Chromosome.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:InterPro.
DR   GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05017; SIS_PGI_PMI_1; 1.
DR   CDD; cd05637; SIS_PGI_PMI_2; 1.
DR   InterPro; IPR019490; Glu6P/Mann6P_isomerase_C.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR035484; SIS_PGI/PMI_1.
DR   NCBIfam; TIGR02128; G6PI_arch; 1.
DR   Pfam; PF10432; bact-PGI_C; 1.
DR   Pfam; PF01380; SIS; 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:ADC89549.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002043}.
FT   DOMAIN          20..153
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   316 AA;  35432 MW;  244DBC4B67238F78 CRC64;
     MQALEWLENM PQQFKKMPVE VVELSPYRGI VFTGMGGSGI VGEITAMFLE RRGVDIPTLV
     VKDYRLPPCV KEGWLVVAVS YSGNTEETLS AVEEAVRRGS TVVSVSSGGK LKNVALQYNL
     PHVDLPQGFA PRYALGYMLS AVLSLMGMGD ISQKMGEHLA SYSSVIKEKA KELAQRLKNY
     LPVVYATPLT GVCAVRYKAQ INENAKTLCH TALLPELHHN EIVGLDNYLT RQMCHFLLLY
     DREDHPRILR RVQITRDILQ EMGLVPIELE GEGESFEERL AYLIYLGDWL SYHLAVLYGF
     DPLPVKSIDR IKGMLS
//
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