ID A0A0Q9QC71_9GAMM Unreviewed; 774 AA.
AC A0A0Q9QC71;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-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=ASG87_12535 {ECO:0000313|EMBL:KRF00519.1};
OS Frateuria sp. Soil773.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Frateuria.
OX NCBI_TaxID=1736407 {ECO:0000313|EMBL:KRF00519.1, ECO:0000313|Proteomes:UP000051919};
RN [1] {ECO:0000313|Proteomes:UP000051919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil773 {ECO:0000313|Proteomes:UP000051919};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF00519.1, ECO:0000313|Proteomes:UP000051919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil773 {ECO:0000313|EMBL:KRF00519.1,
RC ECO:0000313|Proteomes:UP000051919};
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 -!- 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:KRF00519.1}.
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DR EMBL; LMSL01000004; KRF00519.1; -; Genomic_DNA.
DR RefSeq; WP_056000540.1; NZ_LMSL01000004.1.
DR AlphaFoldDB; A0A0Q9QC71; -.
DR STRING; 1736407.ASG87_12535; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000051919; 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 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 321..448
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 467..564
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 569..676
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 706..763
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 774 AA; 83160 MW; EF5C38DB061467CB CRC64;
MQTKMAGRRG SRAQVEWQSL LPLAGGTLLL LLGLFCVWQT WLIAGEGRAV DRVHAAQEQA
VQALAAELAV QRKPVEQAVA ALDPASLQGD RAALLATLRQ RLPQALAVEL YSGGLDEVLH
VNYREFGYAK AAQLMAAQMA DGATPMQTVG AGNGERRLSL ALPLGQAARP VAWLWVELPF
GPLQRRFEAI PAGGGRLDLR QGDDRNEVRL LSHGVASAEA EPAARPVPGS TFTVGAGLPV
AFIVLPRAWP LAALLSLLGL GGGLYLLWLR MHPRVRVEDL SEPEETKLSD VIESKPAPAK
APVRAAAKPP AVSPAEIDPS IFRAYDVRGV VGKSLTSEVA KLLGQSIGTL MREKGLREIV
VGRDGRLSGP ELAGALSEGL RAAGIDVIDV GAAPTPVIYY AAYRFNTGSC VAVTGSHNPP
DYNGFKIVVG GETLSEGAIK DLYRRIAGGT LESGGEGGLR QLDVVPDYIE RIVSDVQAER
SLKVVVDCGN GIPGAVAPQV LEGIGCEVIP LYCEVDGHFP NHHPDPSDPH NLEDLILAVR
QTGADLGVAF DGDGDRLGVV TREGEIVFPD RTLMLFARDV LSRQPGATVI YDVKCTGHLR
GQILEAGGSP LMWRTGHSLI KAKMRETQAE LAGEMSGHFF FKERWYGFDD GIYAGARLLE
ILAGDPEGRT PEQIFATCPK GVSTPELKIE LAEGEHYRFI ERFKEQAQFG DATLVTIDGV
RADWPDGWGL VRASNTTPVL VLRFDADNAA ALKRIQQVFR EQLFAVDPAL KLPF
//
