ID W2UG17_9GAMM Unreviewed; 455 AA.
AC W2UG17;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN Name=algC_1 {ECO:0000313|EMBL:ETN92869.1};
GN ORFNames=U062_00751 {ECO:0000313|EMBL:ETN92869.1};
OS Gammaproteobacteria bacterium MOLA455.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Porticoccaceae.
OX NCBI_TaxID=1411685 {ECO:0000313|EMBL:ETN92869.1, ECO:0000313|Proteomes:UP000018839};
RN [1] {ECO:0000313|EMBL:ETN92869.1, ECO:0000313|Proteomes:UP000018839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOLA455 {ECO:0000313|EMBL:ETN92869.1,
RC ECO:0000313|Proteomes:UP000018839};
RX PubMed=24482511;
RA Courties A., Riedel T., Jarek M., Papadatou M., Intertaglia L., Lebaron P.,
RA Suzuki M.T.;
RT "Draft Genome Sequence of the Gammaproteobacterial Strain MOLA455, a
RT Representative of a Ubiquitous Proteorhodopsin-Producing Group in the
RT Ocean.";
RL Genome Announc. 2:e01203-e01213(2014).
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, 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:ETN92869.1}.
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DR EMBL; AZIN01000001; ETN92869.1; -; Genomic_DNA.
DR AlphaFoldDB; W2UG17; -.
DR STRING; 1411685.U062_00751; -.
DR PATRIC; fig|1411685.3.peg.731; -.
DR eggNOG; COG1109; Bacteria.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000018839; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:RHEA.
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; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR43771:SF1; 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, ECO:0000313|EMBL:ETN92869.1};
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:UP000018839}.
FT DOMAIN 7..132
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 153..258
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 263..373
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 378..454
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 455 AA; 50464 MW; 016DE1701687E84F CRC64;
MTDLTCFKAY DIRGQLGTEL DEEIAYRIGR AYAEFLKPKS IVLGGDMRLT SEALKAALSE
GIRDAGADVI DIGMVGTEEV YFATSFLDAD GGIEVTASHN PIDYNGMKPI REGSRPISSD
TGLLDIKRLA EENNFAPSDP AVRGEYKKLS ILDDYLDHLL GYIDNSAITP LKIVMNAGNG
AAGHVVDAIE TRFAELKLPI EIVKIFNQPD GTFPNGIPNP ILHENRAPTI DAVLEHKADM
GIAWDGDFDR CFLVDEKGNF IEGYYIVGLL AEAFLLKNPG AKIVHDPRLT WNTIDVVNKG
GGEAVQSKTG HAFIKERMRA EDAVYGGEMS AHHYFRDFFY CDSGMIPWLL VMELITRSGK
PLSALVDEMV EAYPSPGEIN RKIADPAAAI QRVREHYQAR ALLVDETDGI SMEFAQWRFN
LRMSNTEPVV RLNLETRGDR DLLAKHQQEL LTLLD
//
