ID A0A1Y1R229_9GAMM Unreviewed; 925 AA.
AC A0A1Y1R229;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=B0D91_13285 {ECO:0000313|EMBL:OQX33986.1};
OS Oceanospirillales bacterium LUC14_002_19_P2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales.
OX NCBI_TaxID=1940822 {ECO:0000313|EMBL:OQX33986.1, ECO:0000313|Proteomes:UP000192421};
RN [1] {ECO:0000313|EMBL:OQX33986.1, ECO:0000313|Proteomes:UP000192421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LUC14_002_19_P2 {ECO:0000313|EMBL:OQX33986.1};
RA Lim S.J., Davis B.G., Gill D.E., Engel A.S., Anderson L.C., Campbell B.J.;
RT "Novel co-symbiosis in the unique lucinid bivalve Phacoides pectinatus.";
RL Submitted (FEB-2017) 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}.
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:OQX33986.1}.
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DR EMBL; MUIA01000378; OQX33986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1R229; -.
DR Proteomes; UP000192421; 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:UP000192421};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 475..604
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 623..717
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 722..828
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 837..915
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 355..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 925 AA; 101185 MW; B5B57777F591C7A1 CRC64;
MAGSSIFNNK NRYRDNAVKG FFGKARASNR RSHSASDTPE SQPLSYPTPL IAIGVLLLLG
LFSALYVWQT HVKARATAEQ QANQFGQHMA DVLSRELRLM QNSTDHMATL SPVAEALQSQ
DTAQLADLRS LLRGSLPDAI NLQLNPANQP IGQDTSFAAR EMIRRSQRGQ TVTPEAASTQ
QQWVINTVSP VIINNERLGT LLVAYDLQRL QNALKLSDAT LGQWQLLQTI DGPARELVRA
GTTPASDSTI LKYSLTQTGW KLTFQPSSHW VASHQPSLVF LLITLGAIMV VPVLLDRFWR
SQNHRLMGDN YLLKTLICDI SDGRNPQIGD YKVAIFREIA QNILNTATAS KIDQYRQAST
TPLASPPTPE VYYDPLDEPQ AHQTTVTVEQ PSSTQPLPPK DDITDASDDP FAAPLFQDND
LLELSLADHE SPDTLTTPTD GMTTGEESSP VSNTEQPDTV TAPTPHPATT VPASIFRAYD
IRGVVGDELT PDTVELLGRA IGTEALARGE TTLIVGMDGR LSSPALRDQL VAGITGSGCD
VITIGTVPTP VLYYATHELA ARSGVMITGS HNPPQYNGFK IVLTGETLAN DAIQGLYQRI
SKQALNSGEG QVTEHDVLGD YHQRILDDII IQRPLKVVID CGNGVAGVIA PELFEALGCE
VIPLYCDVDG NFPNHHPDPG NPDNLQDIVA KIAETGADLG LAFDGDGDRV GLVTNQGRII
FPDRLLMLLA KDIVTRNPGC DVIYDVKCTR RLNSLISSYG GRPMMWKTGH SLIKAKMKET
GALLAGEMSG HIFLKERWYG FDDGIYSAAR LVEILSAQTL STDEVFDSFP DSVNTPEINI
QVTDENKFSL IEQFANKGQF KEGNVITIDG VRVEFPWGWG LVRASNTTPV LVLRFEADDN
QHLDRIKTLF REQLKAVDNT LPVNF
//
