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Database: UniProt
Entry: D2SFK6_GEOOG
LinkDB: D2SFK6_GEOOG
Original site: D2SFK6_GEOOG 
ID   D2SFK6_GEOOG            Unreviewed;       454 AA.
AC   D2SFK6;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ADB76860.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:ADB76860.1};
GN   OrderedLocusNames=Gobs_4298 {ECO:0000313|EMBL:ADB76860.1};
OS   Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / KCC
OS   A-0152 / KCTC 9177 / NBRC 13315 / NRRL B-3577 / G-20).
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=526225 {ECO:0000313|EMBL:ADB76860.1, ECO:0000313|Proteomes:UP000001382};
RN   [1] {ECO:0000313|EMBL:ADB76860.1, ECO:0000313|Proteomes:UP000001382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC   NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RX   PubMed=21304698;
RA   Ivanova N., Sikorski J., Jando M., Munk C., Lapidus A., Glavina Del Rio T.,
RA   Copeland A., Tice H., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Meincke L.,
RA   Brettin T., Detter J.C., Detter J.C., Rohde M., Goeker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT   "Complete genome sequence of Geodermatophilus obscurus type strain (G-
RT   20).";
RL   Stand. Genomic Sci. 2:158-167(2010).
RN   [2] {ECO:0000313|Proteomes:UP000001382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC   NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M.,
RA   Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Geodermatophilus obscurus DSM 43160.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
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DR   EMBL; CP001867; ADB76860.1; -; Genomic_DNA.
DR   RefSeq; WP_012950285.1; NC_013757.1.
DR   AlphaFoldDB; D2SFK6; -.
DR   STRING; 526225.Gobs_4298; -.
DR   KEGG; gob:Gobs_4298; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_9_2_11; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000001382; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03089; PMM_PGM; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR   InterPro; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ADB76860.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001382}.
FT   DOMAIN          8..124
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          157..256
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          265..369
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          375..452
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   454 AA;  48995 MW;  AE188637F9489314 CRC64;
     MRNLSVIIKA YDVRGVVPDE WDEGIARRIG AAFAELVWQE SGATAVVTAH DMRDSSVPLS
     RAFAEGVLSR GVDVVEAGLG STDLLYFASG SLGVPGAMFT ASHNPAQYNG IKLCRAGATP
     VGQESGLATL REWAERDSYD RVPDRTASIN QRDLLAEYAA HLRSLVDLSA IRPLRVVVDA
     GNGMGGHTVP VVLAGLPLEV LPLYFELDGS FPNHEANPLD PANLVDLQAE VRRTGADIGL
     AFDGDADRVF VVDERGEAVS PSAVTALVAV RELAKGRGTT VIHNLITSRA VPEIVREHGG
     EPVRTRVGHS FIKAEMARTD AVFGGEHSAH YYFRDFWRAD TGMLAAMHVL AALGEQSRPL
     SELTAGYSRY AASGEINSTV ADAAGRTRAV RETFEEQDGV TVDELDGLTV DLPDGSWFNL
     RASNTEPLLR LNVEAPDEAR MTRLRDRVLE MVRA
//
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