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Database: UniProt
Entry: G1WKA3_9ACTN
LinkDB: G1WKA3_9ACTN
Original site: G1WKA3_9ACTN 
ID   G1WKA3_9ACTN            Unreviewed;       464 AA.
AC   G1WKA3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Phosphoglucomutase/phosphomannomutase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF9452_01723 {ECO:0000313|EMBL:EGX69432.1};
OS   Collinsella tanakaei YIT 12063.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae; Collinsella.
OX   NCBI_TaxID=742742 {ECO:0000313|EMBL:EGX69432.1, ECO:0000313|Proteomes:UP000004830};
RN   [1] {ECO:0000313|EMBL:EGX69432.1, ECO:0000313|Proteomes:UP000004830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 12063 {ECO:0000313|EMBL:EGX69432.1,
RC   ECO:0000313|Proteomes:UP000004830};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Collinsella tanakaei YIT 12063.";
RL   Submitted (JUN-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}.
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:EGX69432.1}.
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DR   EMBL; ADLS01000023; EGX69432.1; -; Genomic_DNA.
DR   RefSeq; WP_009141757.1; NZ_JH126472.1.
DR   AlphaFoldDB; G1WKA3; -.
DR   STRING; 742742.HMPREF9452_01723; -.
DR   GeneID; 62759416; -.
DR   PATRIC; fig|742742.3.peg.1706; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_7_1_11; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000004830; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR   PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
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:UP000004830}.
FT   DOMAIN          7..136
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          154..254
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          259..366
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          414..454
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   464 AA;  50698 MW;  C00BFED77BD04712 CRC64;
     MSAIIHFEAD GWRARTDGDF TEENVVRIAD AAGEYWNRRN PGAMVYVCYD ARPGAEECAK
     AAARTLAAHG VAAVLSDRVA PTPALTWAVS RNSRVCGGFA VTGSHYPYDY LGVKLCNADG
     GTGCPDFIEE IEHLIEPEVY GVREHYAIKD FVTPYFDYLS TLVDGDAIAR ARLRVVYDPM
     YGAARTYMPQ LLGALGVEVE EIHGADDEGW RDVRPEPIEP WVDDCEQAVV ECAAHAGLIN
     DGDAARVGAV DEYGNYVSPQ KIMALVLGHL VINRGMTGRV VVNQATSVLA RRVAQSLGCK
     VTVRPIGFTY IYEEMRKGGV LLGGEGSGGF AIPSHVAERD GLLVNVLLCE LMATTGKKLG
     ELVNELEMNF GRLWYGRRDV RVRVEQVEML RTIMPGLNPE LVGGRKPVAV SHMDGLRFEF
     QDESWLLLRP SASESVVRVY AEAPSVEIRD ELLDAGADMA KGNA
//
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