ID A0A0U4HLT1_9PSED Unreviewed; 853 AA.
AC A0A0U4HLT1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=APT59_21610 {ECO:0000313|EMBL:ALZ86682.1};
OS Pseudomonas oryzihabitans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=47885 {ECO:0000313|EMBL:ALZ86682.1, ECO:0000313|Proteomes:UP000064137};
RN [1] {ECO:0000313|EMBL:ALZ86682.1, ECO:0000313|Proteomes:UP000064137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA-ARS-USMARC-56511 {ECO:0000313|EMBL:ALZ86682.1,
RC ECO:0000313|Proteomes:UP000064137};
RA Harhay G.P., Harhay D.M., Smith T.P.L., Bono J.L., Heaton M.P.,
RA Clawson M.L., Chitko-Mckown C.G., Capik S.F., DeDonder K.D., Apley M.D.,
RA Lubbers B.V., White B.J., Larson R.L.;
RT "Annotation of Pseudomonas oryzihabitans USDA-ARS-USMARC-56511.";
RL Submitted (JAN-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; CP013987; ALZ86682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U4HLT1; -.
DR KEGG; por:APT59_21610; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000064137; Chromosome.
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:UP000064137};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 403..531
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 548..645
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 650..754
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 765..842
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 853 AA; 91906 MW; 1D256CA6BCA5D9F2 CRC64;
MARGKNGKDV RKTAPRVAAL PGMGAGLLLA LAGLLLAAML LWFLVLQPQG ARNQEQQADQ
ALQAQATSLN QLLVGLTRRL QGVAGDALVL QALQGDDPAA RAAAESQLRQ RLGVVDVLVV
PAGMRQIEDD RPGPLNYAAL DLLKRLESGQ RTPPEAYRVG DRWLVYSAQP IRRGDQLLGS
AVLVEELPAV LQGWATPPAT VGQWRLLQQF PGGGVQVLAS GGTPGDPALM RRLATGSPLW
TLELAPAAEA GADTPVGIPL VALLLALFGL LAGFWLFSRE LSRRLRDDVR SLTAYAEELE
SNQIAKSPTL RLAVMEPVAK STARLANRSA GSSPDLYAAA PSDAVAKTLA EFADRGRAQQ
SEPLFQTTDI LDISILDEDQ DLLGLEKPPM STTPQAPQLN ASIFRAYDIR GVVGDSLTAE
AAYWIGRAIG SESLARGEPN VAVGRDGRLS GPELVAQLIK GVADSGANVS DVGMVPTPVL
YYAANVLEGK SGVMLTGSHN PPDYNGFKIV IAGETLANES IQRLRERIET GEVASGQGQI
KQVDVLKSYA DYIRNDVVLA KKLKVVVDAG NGVAAVNAPQ LIESLGCEVI PLFCEVDGNF
PNHHPDPGKP ENLEDLIAKV KETGADLGLA FDGDGDRVGV VTNEGKIIYP DQLLMLFAKD
VVSRNPGADI IFDVKCTRRL NNLIAGYGGR PIMWKTGHSL IKKKMKETGA LLAGEMSGHV
FFKERWFGFD DGIYSAVRLL EILSQEKSSA QQVFDTFPVD ISTPEINIQV TEENKFGIIE
TLQRDAQWGD AQITTLDGVR VDYQHGWGLV RASNTTPVLV LRFEAETLEE LERIKTVFRK
QLLAVQPDLN LPF
//
