ID H1Q3W4_9BACT Unreviewed; 581 AA.
AC H1Q3W4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Phosphoglucomutase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9140_01602 {ECO:0000313|EMBL:EHO68562.1};
OS Prevotella micans F0438.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=883158 {ECO:0000313|EMBL:EHO68562.1, ECO:0000313|Proteomes:UP000016023};
RN [1] {ECO:0000313|EMBL:EHO68562.1, ECO:0000313|Proteomes:UP000016023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0438 {ECO:0000313|EMBL:EHO68562.1,
RC ECO:0000313|Proteomes:UP000016023};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA Blanton J.M., Wade W.G., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella micans F0438.";
RL Submitted (DEC-2011) 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, ECO:0000256|RuleBase:RU004326}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHO68562.1}.
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DR EMBL; AGWK01000042; EHO68562.1; -; Genomic_DNA.
DR RefSeq; WP_006953108.1; NZ_JH594522.1.
DR AlphaFoldDB; H1Q3W4; -.
DR STRING; 883158.HMPREF9140_01602; -.
DR PATRIC; fig|883158.3.peg.1604; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_0_10; -.
DR Proteomes; UP000016023; Unassembled WGS sequence.
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; cd05799; PGM2; 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; 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 PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000016023}.
FT DOMAIN 52..189
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 214..318
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 328..450
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 581 AA; 66039 MW; DC303A8C5C388FB8 CRC64;
MENNQKLIAQ CEAKAREWLS PAFDETTKKK VQNMLENPDK NELIESFYKD LEFGTGGLRG
IMGAGSNRMN IYTVGMATQG FANYLKKNFK DKEQISVVVC YDCRNNSRLF AETVADIFSG
NGIKVYLFED MRPTPECSFA IRHFKAQAGV NMTASHNPRE YNGYKAYWED GAQVLSPHDT
GIIDEVNKVK VEDICFEARP ELIQIIGKEI DQIYLEEIKT LCIDPEVITH QHDLKIVYTP
LHGAGMKLIP QSLNLWGFNN IHCVKEQMVK DGNFPTVDRP NPEFAEALTL ALRDAKAIDA
DILMASDPDA DRVGMACKND KGEWVLINGN QTCLLFLWYI ITNRQAVGKM QPSDFIVKTI
VTTEVIAEIA RKQHIEMRDC YTGFKWIARE IALSEGKQKY IGGGEESYGF LAEDFVRDKD
AVSACSLLAE MCAYAKDHGK TLYNILMEIY IEYGYSKEHT VNVERPGKSG AEEIQQMMKN
FRINPPQQLG GSRICVWKDY QTLEETHDDG SKHKLEMPDT SNVLQWFCED GTKVSVRPSG
TEPKIKFYLE IKDKMNSPVD YTECEKRAEQ KIEKIKKDLG V
//
