ID Q3Z945_DEHM1 Unreviewed; 475 AA.
AC Q3Z945;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase family protein {ECO:0000313|EMBL:AAW40241.1};
GN OrderedLocusNames=DET0510 {ECO:0000313|EMBL:AAW40241.1};
OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS (Dehalococcoides ethenogenes (strain 195)).
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=243164 {ECO:0000313|EMBL:AAW40241.1, ECO:0000313|Proteomes:UP000008289};
RN [1] {ECO:0000313|EMBL:AAW40241.1, ECO:0000313|Proteomes:UP000008289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195
RC {ECO:0000313|Proteomes:UP000008289};
RX PubMed=15637277; DOI=10.1126/science.1102226;
RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA Ward N.L., Nelson W.C., Deboy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA Zinder S.H., Heidelberg J.F.;
RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT ethenogenes.";
RL Science 307:105-108(2005).
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, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; CP000027; AAW40241.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3Z945; -.
DR STRING; 243164.DET0510; -.
DR KEGG; det:DET0510; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_1_0; -.
DR InParanoid; Q3Z945; -.
DR Proteomes; UP000008289; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05800; PGM_like2; 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; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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; 2.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 5..137
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 166..267
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 274..381
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 421..468
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 475 AA; 51672 MW; C8DDDF5158C52EAD CRC64;
MTSQIKFGTD GWRGIIAKDF TFDNVSVCAQ ATAAYLKNTS PRNLSLVIGY DTRFASADFA
RSAAEVMAAN GIKVYFCSCP TPTPVISHGV VNLKAAGAVI ITASHNPARW NGFKVKSADG
ASAPTQMITG IEAEIAKLGD KPPVLNLDFD TAVSRGLIEH VDLAPAYFEK IGGLVDIEKL
RDAGFNIAID SMHGAGIGYF KQLLDGGCNR LNEINAEPNP NFPGMLQPEP ITPNLAKLMR
LVKDIRSDIG LATDGDSDRL GVVDEMGNFL NQLQVFSLLA LYMLEVKGLR GPLVKTITNS
SMIDKLGELY NVPVFETKVG FKYVSPVMLE QNALIGGEES GGYAFTGHVP ERDAILAGAY
FLDFMITTGK SPAEMLEYLY SKVGPHYYNR VDYTFAEARR EEIIKHLTDQ KPASLGETKV
VSTDKLDGFR YKLEDGSWLL IRFSGTEPLL RVYAESPSQA KTAALLEDGR QLSGI
//
