ID A0A0Q4G334_9SPHN Unreviewed; 461 AA.
AC A0A0Q4G334;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:KQM68016.1};
GN ORFNames=ASE75_03925 {ECO:0000313|EMBL:KQM68016.1};
OS Sphingomonas sp. Leaf17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735683 {ECO:0000313|EMBL:KQM68016.1, ECO:0000313|Proteomes:UP000051777};
RN [1] {ECO:0000313|EMBL:KQM68016.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM68016.1,
RC ECO:0000313|Proteomes:UP000051777};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM68016.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM68016.1,
RC ECO:0000313|Proteomes:UP000051777};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQM68016.1}.
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DR EMBL; LMKL01000001; KQM68016.1; -; Genomic_DNA.
DR RefSeq; WP_055928937.1; NZ_LMKL01000001.1.
DR AlphaFoldDB; A0A0Q4G334; -.
DR STRING; 1735683.ASE75_03925; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000051777; 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; 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, 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:UP000051777}.
FT DOMAIN 10..124
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 168..250
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 254..362
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 370..447
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 461 AA; 49087 MW; 1E1013A82A0573BB CRC64;
MRHVFDPSVL REYDIRGTVG RTLGTADATA IGRSFATRLR RAGGRRVVVG YDGRTSSPAL
EAALVAGLTA SGVDVVRIGM GPSPMLYHAE ATLEVDGGIQ ITGSHNPADD NGFKMIIGHA
SFFGADIHDL ARLAAAGDWE EGSGDVTQAD VMDLYVGRLM AGYGGGAYRI GWDAGNGASG
PVIETLVQML PGDHHLLFTE VDGRFPNHHP DPTQEPNLAD LKRLVIEKSL DFGFAFDGDG
DRIGAVDGSG RVVWGDQLLA ILAEPVLREL PGATIIGDVK SSQGLFDRVR DLGGVPLMWK
TGHSLMKTKM QETGAPLGGE ISGHMFFGHE YYGFDDAHYA AVRLIRAIHL SGQSLAALHD
ALPAWINTPE IQIRVGSQDK FAVMAGILDR LAASDAVVDR TDGARVTTED GWWLLRASNT
QDVLTARAEA RDAAGLARLL DAVDAHLVAV GLEPARRPAH G
//
