ID A0A077M605_9MICO Unreviewed; 575 AA.
AC A0A077M605;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Putative phosphomannomutase {ECO:0000313|EMBL:CCI51984.1};
GN ORFNames=BN13_1370002 {ECO:0000313|EMBL:CCI51984.1};
OS Tetrasphaera jenkinsii Ben 74.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1193518 {ECO:0000313|EMBL:CCI51984.1, ECO:0000313|Proteomes:UP000035720};
RN [1] {ECO:0000313|EMBL:CCI51984.1, ECO:0000313|Proteomes:UP000035720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ben 74 {ECO:0000313|EMBL:CCI51984.1,
RC ECO:0000313|Proteomes:UP000035720};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCI51984.1}.
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DR EMBL; CAJC01000043; CCI51984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077M605; -.
DR STRING; 1193518.BN13_1370002; -.
DR Proteomes; UP000035720; 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 CDD; cd03089; PMM_PGM; 1.
DR Gene3D; 2.20.25.10; -; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 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 SUPFAM; SSF158997; Trm112p-like; 1.
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:UP000035720}.
FT DOMAIN 9..136
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 178..268
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 295..385
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 394..476
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 575 AA; 60343 MW; 39E8CB7E01BC65B8 CRC64;
MSPRDLTDIV KAYDVRGLVP SQFDSDVARA LGTAFAEIIA RPEGAYAVVI GHDMRASSPE
LSGAFAEGAR SVGVDTIEIG LASTDGLYFA SGILNLPGAM FTASHNPAAY NGIKLTRAGA
RPVGQDTGLT AIRERAAALL ADPSAATPAD QPGSGDRRDV LADYGTFLRG LVDLRGIRPL
KVVVDAANGM AGMTVPAVLG TAAGLEPLPL DIVPLYFELD GTFPNHEANP LDPANLVDLQ
RAVVEHGADL GLAFDGDADR CFVVDERGEP VSPSAVTGLV AEREIDKEVA SGVDPASVHI
VHNVISSAAV PELIRAKGAV PVRTRVGHSF IKAEMASAGA VFGGEHSAHY YFRDFWFADT
GMLAAFHVLA ALGEQDAPLS ALVADYGPYA ASGEINSTIT DTPAAVERVR AWASAQGLVG
EEMDGLTITH SAVEDAPMWW LNLRASNTEP LLRLNVEAAD SETMARVRDE VLALVRADDN
AAAASNPNVT PVNPNTDPAN AVAAISANPG DTPVDTGIEP WVRELLRCPA CRSELRDVRE
GGILELACTG SECRRIYPIT DGIPVLLIDE ARIGD
//
