ID A0A1H6T1N4_9GAMM Unreviewed; 773 AA.
AC A0A1H6T1N4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=SAMN04487997_1646 {ECO:0000313|EMBL:SEI73978.1};
OS Frateuria terrea.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Frateuria.
OX NCBI_TaxID=529704 {ECO:0000313|EMBL:SEI73978.1, ECO:0000313|Proteomes:UP000199420};
RN [1] {ECO:0000313|EMBL:SEI73978.1, ECO:0000313|Proteomes:UP000199420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26515 {ECO:0000313|EMBL:SEI73978.1,
RC ECO:0000313|Proteomes:UP000199420};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC EC=5.4.2.8; Evidence={ECO:0000256|ARBA:ARBA00000586};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 2/2. {ECO:0000256|ARBA:ARBA00004699}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; FNYC01000002; SEI73978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6T1N4; -.
DR STRING; 529704.SAMN02927913_1561; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000199420; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd03089; PMM_PGM; 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; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR43771; 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 PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199420};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 320..448
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 466..563
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 568..673
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 686..762
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 289..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 82574 MW; E062B656A0A8ABA0 CRC64;
MARKIAREPG AGGAVAWQQL LPLAGGTVLL LLGLFCAWQT WLIASESGGV ARVHAAQDAA
VRSLAAEIAG ERKQVAQAAA SLDPSMLQGD RAQLAQALRE RLPQALGVDV YSAGLDEVLH
ANYRTFGYAK AAQLMAAQTG EGEPPMQTVV AGGQRRLSLV QPLGSAQRPQ GWAWIELPFT
PLQQRFESIA PGDGRIDLRQ GDDRGELSLL TRGAPSAQAE DIAKPVPGSS FSVRAALPAA
FILLPRFWPL AALLALLCIG GGLYLLSLRG RTPVREEIQP EETMVSDVIP AKPQPAPPAA
RPAASMPPAA SPADAVDPSI FRAYDVRGVV GKTLTAQVAR LLGQSIGTLM REKGLNEIVV
GRDGRLSGPE LAGALSDGLR EAGIDVIDVG AVPTPVVYFA AYRFNTGSGV AVTGSHNPPD
YNGFKIVVGG ETLSEGAIQD LYKRIASGAL EAGGQGGLRH VDVVPDYIER ITSDVQAERR
LKVVVDCGNG IPGAVAPQVL EGIGCEIVPL YCEVDGTFPN HHPDPSDPHN LEDLIHAVRQ
TGADLGVAFD GDGDRLGVVT REGEIIYPDR LLMLFARDVL SRQPGATIIY DVKCTGHLKG
QVLEAGGSPL MWRTGHSLIK AKMRQTQAEL AGEMSGHFFF KERWYGFDDG IYAGARLLEI
LASDLDARTP EQIFATCPKG VSTPELKIEL AEGEHYRFIE KFKEKAGFGD ATLTTIDGVR
ADWPDGWGLV RASNTTPVLV LRFDADNAAA LKRIQQAFRE QLFLVDPGLK LPF
//
