ID G4SUK7_META2 Unreviewed; 846 AA.
AC G4SUK7;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN OrderedLocusNames=MEALZ_0132 {ECO:0000313|EMBL:CCE21833.1};
OS Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM
OS B-2133 / 20Z) (Methylomicrobium alcaliphilum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylotuvimicrobium.
OX NCBI_TaxID=1091494 {ECO:0000313|EMBL:CCE21833.1, ECO:0000313|Proteomes:UP000008315};
RN [1] {ECO:0000313|Proteomes:UP000008315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
RC {ECO:0000313|Proteomes:UP000008315};
RX PubMed=22207753; DOI=10.1128/JB.06392-11;
RA Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., Lajus A.,
RA Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., Dispirito A.A.,
RA Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., Barbe V., Medigue C.,
RA Trotsenko Y.A., Kalyuzhnaya M.G.;
RT "Genome sequence of the haloalkaliphilic methanotrophic bacterium
RT Methylomicrobium alcaliphilum 20Z.";
RL J. Bacteriol. 194:551-552(2012).
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; FO082060; CCE21833.1; -; Genomic_DNA.
DR RefSeq; WP_014146651.1; NC_016112.1.
DR AlphaFoldDB; G4SUK7; -.
DR STRING; 1091494.MEALZ_0132; -.
DR KEGG; mah:MEALZ_0132; -.
DR PATRIC; fig|271065.3.peg.136; -.
DR HOGENOM; CLU_013562_0_1_6; -.
DR Proteomes; UP000008315; 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:UP000008315};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 394..523
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 541..638
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 643..751
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 778..835
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 366..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 846 AA; 92211 MW; 00C6D2789F7CD64C CRC64;
MERIFLPLSI IAAFVVLLTG GAIYWANDSS IKEAKHDSAM ALAAGTALGI SKQIEQLASA
IDKMARDPTV IEAMENRDRG RIRALEAQLE KYLPGALKIR LLLPGINDLD TEHVPHMGFA
DLDMVKETFS GNPQPLIQGE GANRHLAITA RIEESGRVAG VILASLSYDF INNSIKPSSI
GNQLIQLRQG DFELAAVGNR ALIGDAASVQ MPIAHTAWQV QVWYQIGGSS SDVGLIAAIM
LIAVLLVCLA FFVGYRKSAN ILSHDQSIVL KAVKDLMTGN AYGNYPVNLS EMSVIISTLV
QFKRVLDHQG DDVVAIANES EADFDGFFEE SDFAIEEIVE NAKAGDAETS PVSMPDVDWD
MPIPEAKPTP VPEQPKPSPI SKATAPLHEG SGEVFRAYDI RGVVGKTLTT ELAYDIGRAF
GTEVRKADCN IVVVGRDGRH SSPELADAVI NGIVSTGRDV LDLGMVPTPI LYFVTQHTEG
RTGLMITGSH NPAEYNGMKM VIKGETLAGQ RVAKLKNIID KQDYAVEVGG TVDQNSMFVN
EYIGIVAEDV HLVRPMKIVL DCGNGVAGDI APILFKTLGC EVVELFCDVD GSFPNHHPDP
SVPENLEDLI AAVQHYEADI GIAFDGDGDR LGVVDSNGKI IWPDRLMMLF AKDVLARKPG
AQIVYDVKCS RHLAEQIAKY GGRALMWKTG HSYMKAKVKE TGAKLAGEMS GHIFFNDRWY
GFDDALYSAA RLIEILSSDA RTSAEIFAEF PESLNTPELL VSMKEGENFD FIERLFAKAD
FKDGKITNID GLRVDFSDGW GLVRASNTTP SLVVRFEADS EQAMRRIQKE FKTLIASIEP
QLVLPF
//
