ID K0YNH0_9ACTO Unreviewed; 562 AA.
AC K0YNH0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:EJZ84958.1};
GN ORFNames=HMPREF9240_01855 {ECO:0000313|EMBL:EJZ84958.1};
OS Winkia neuii BV029A5.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Winkia.
OX NCBI_TaxID=888439 {ECO:0000313|EMBL:EJZ84958.1, ECO:0000313|Proteomes:UP000006075};
RN [1] {ECO:0000313|EMBL:EJZ84958.1, ECO:0000313|Proteomes:UP000006075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BVS029A5 {ECO:0000313|EMBL:EJZ84958.1,
RC ECO:0000313|Proteomes:UP000006075};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinomyces neuii subsp. anitratus BVS029A5.";
RL Submitted (JUL-2012) 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:EJZ84958.1}.
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DR EMBL; AGWP01000010; EJZ84958.1; -; Genomic_DNA.
DR AlphaFoldDB; K0YNH0; -.
DR PATRIC; fig|888439.3.peg.1863; -.
DR eggNOG; COG0033; Bacteria.
DR HOGENOM; CLU_016950_8_1_11; -.
DR Proteomes; UP000006075; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05801; PGM_like3; 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; IPR045244; PGM.
DR InterPro; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
DR PANTHER; PTHR22573:SF57; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 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 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006075}.
FT DOMAIN 44..191
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 221..335
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 338..458
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 502..557
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 562 AA; 59991 MW; 642AF60E381B22D8 CRC64;
MHNRSMHERA GTKATPADLI NVDEVLSAYY DIVPDPNNPD QQVVFGTSGH RGSSLDGAFN
EAHIVATTAA IVEYRKEHGI NGPLFIGRDT HALSEPAWRT ALQVLVAAGV TVRIDSRDSY
TPTPAVSHAI LHANGANSRH GVRTDGNGLA DGIVVTPSHN PPRDGGFKYN PPTGGPADTD
ATGPIADRAN ELLADWQSIP RIPADEVLSD AHVERYDYLG SYVDDLASII DMDAIRDAGI
RIGADPLGGA SVDYWAAIAE KYALDLTVVN PTVDPTWSFM TLDWDGKIRM DCSSPSAMAS
LLNAMTPDKD GHTPYDIATG NDADSDRHGI VTADGLMNPN HYLAVAIEYL YTHRPQWSAD
CAVGKTLVSS RLIDQVAANL GRNLIEVPVG FKYFVPGLLD GSIGFGGEES AGASFLRRNG
EVWSTDKDGI IMALLASEIL AVTGKTPSQL HKEQVERFGK PSYARVDAAA TKEQKAKLKA
LSPQDVAADE LAGEPITAKL VKAPGNDAPI GGLKVTTRNA WFAARPSGTE DVYKVYAESF
LGDDHLKQVQ AAAQEVVAAA LK
//
