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Database: UniProt
Entry: A0A3M2HHB9_9GAMM
LinkDB: A0A3M2HHB9_9GAMM
Original site: A0A3M2HHB9_9GAMM 
ID   A0A3M2HHB9_9GAMM        Unreviewed;       785 AA.
AC   A0A3M2HHB9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE            EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN   ORFNames=EBB59_10775 {ECO:0000313|EMBL:RMH89106.1};
OS   Lysobacter pythonis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=2483112 {ECO:0000313|EMBL:RMH89106.1, ECO:0000313|Proteomes:UP000275012};
RN   [1] {ECO:0000313|EMBL:RMH89106.1, ECO:0000313|Proteomes:UP000275012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4284/11 {ECO:0000313|EMBL:RMH89106.1,
RC   ECO:0000313|Proteomes:UP000275012};
RA   Hans-Juergen B., Huptas C., Sandra B., Igor L., Joachim S., Siegfried S.,
RA   Mareike W., Peter K.;
RT   "Proposal of Lysobacter pythonis sp. nov. isolated from royal pythons
RT   (Python regius).";
RL   Submitted (OCT-2018) 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:RMH89106.1}.
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DR   EMBL; RFLY01000016; RMH89106.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2HHB9; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000275012; 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: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; 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: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.
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:UP000275012};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        241..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          334..463
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          482..579
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          584..688
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          700..774
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   785 AA;  83175 MW;  2292996817A01C0A CRC64;
     MAIKINRQSL PKLQMGSPEE ARRALTLMAV LCGLLALWFM WSGLRLWWAQ AADEALMFER
     DRVAGEIGHQ FGALSAQVVE AVAKPEVAEA LKAGDREAAA ALTAALPKAA AVEVYPADLG
     AFYDKLPETG YGKLAVVEEV QMAGKPVMRV GRSGAGGMLL AGVPLPEGAA ALAAFPLTEA
     NRLIATVKTG NGYIALRQGM VNVIQDGDPA LAGTSEANAA PVRGGGFRIA IGLPTAEAGP
     YGLGALACGA IGLLLAIVAG LLLAWPRLNR RRPAAVVDEA EAPTLGETLA AAPLTQAEGR
     GRVSLADRMG MEEIEMSQDS NVAAGLAPER LDRDIFRAYD IRGVVGQGLD AEVARAIGQA
     VGSLMREQGL SDIVVGRDGR LSGPALSAAL IEGLRSTGRK VIDIGLAPTP LVYFAAYHLR
     AGSCVAVTGS HNPPDYNGFK IVVGGETLSG EAIVALYQRI VEGRLYRAAG PGALETRDAA
     GDYLQRVAAD IQLGRPLRVV VDAGNGAAGD LGPKVLEAIG AEVEPLYCEI DGHFPNHHPD
     PSDPHNLADL TQAVQRSGAD IGLAFDGDGD RLGVVTPAGR NVFPDRLLML FAADVLERQP
     GAVIVYDVKC TGALMPWVLR HGGSPLMWKT GHSFIKAKMR ETDAELAGEM SGHFFFKERW
     YGFDDGIYSA ARLLEILAAR TDDADTVFAG IPEGISTPEL KIPVEDPHAF IERFVAMGDF
     AEARSNTIDG LRADWKNGWG LVRASNTTPI LVLRFEAVDE PALREIQEAF RERLLALEPA
     LDIPF
//
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