ID D4TYH1_9ACTO Unreviewed; 568 AA.
AC D4TYH1;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II {ECO:0000313|EMBL:EFF80059.1};
GN ORFNames=HMPREF0970_00996 {ECO:0000313|EMBL:EFF80059.1};
OS Schaalia odontolytica F0309.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=649742 {ECO:0000313|EMBL:EFF80059.1, ECO:0000313|Proteomes:UP000003150};
RN [1] {ECO:0000313|EMBL:EFF80059.1, ECO:0000313|Proteomes:UP000003150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0309 {ECO:0000313|EMBL:EFF80059.1,
RC ECO:0000313|Proteomes:UP000003150};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2009) 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:EFF80059.1}.
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DR EMBL; ACYT02000028; EFF80059.1; -; Genomic_DNA.
DR AlphaFoldDB; D4TYH1; -.
DR PATRIC; fig|649742.3.peg.720; -.
DR HOGENOM; CLU_016950_0_2_11; -.
DR Proteomes; UP000003150; 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; 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; 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}.
FT DOMAIN 61..203
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 225..326
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 341..445
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 505..536
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 19..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 59344 MW; 6A9F5D366C10FAF5 CRC64;
MPSWQDWRTE TMELLERARQ WASHDPDPAT ASALSSDIEA AERGDEEAAA RVGAAMNGPL
QFGTAGLRGV VGTGESRMNL AVVIRATAGL CEVVKRHATG TPTLVVGCDA RYGSSEFATA
ACRVASAAGV RVLALPQANP TPLTSFAVRH FGADVGVMVT ASHNPAPDNG YKVYLGGSVV
TGDGQGVQIV PPFDAEIAEA IKATPPADQV PMNDDLIEAV DPRDEYVACA SALASGEASA
REDLRIVLTA MHGVGAAITS RVLAEAGFSN VSLVAAQTDP DPDFPTVPFP NPEEAGALDM
AIEQAREEGA DLIIAVDPDA DRCALAVPDP TSETGWSPLS GDQIGSLLGE FLAARGMTGS
LANSIVSSRL LSRIARAHGL EHHTTLTGFK WIARAPGLGF GYEEAIGFCP DPGNVRDKDG
IATSVVAASL VAALKAQGRS VWDELERLAR LHGLHVSSPL TFRVEQIEQI ASGMARLRAQ
PPSVLAGSPV VEVSDLSQGY RGLPPTDGVL VLTEAGDRVI ARPSGTEPKL KCYLEVILPV
AEGEPLPCEQ ARERLDAIKG AFAEIIGL
//
