ID A0A0A0F0P8_9GAMM Unreviewed; 782 AA.
AC A0A0A0F0P8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=N799_05120 {ECO:0000313|EMBL:KGM56170.1};
OS Lysobacter arseniciresistens ZS79.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=913325 {ECO:0000313|EMBL:KGM56170.1, ECO:0000313|Proteomes:UP000029989};
RN [1] {ECO:0000313|EMBL:KGM56170.1, ECO:0000313|Proteomes:UP000029989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS79 {ECO:0000313|EMBL:KGM56170.1,
RC ECO:0000313|Proteomes:UP000029989};
RX PubMed=26516404; DOI=10.1186/s40793-015-0070-5;
RA Liu L., Zhang S., Luo M., Wang G.;
RT "Genomic information of the arsenic-resistant bacterium Lysobacter
RT arseniciresistens type strain ZS79(T) and comparison of Lysobacter draft
RT genomes.";
RL Stand. Genomic Sci. 10:88-88(2015).
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:KGM56170.1}.
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DR EMBL; AVPT01000015; KGM56170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0F0P8; -.
DR STRING; 913325.N799_05120; -.
DR eggNOG; COG1109; Bacteria.
DR Proteomes; UP000029989; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000029989};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 330..458
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 476..574
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 579..686
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 694..771
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 782 AA; 81704 MW; 0FDA98BF6E2A2B93 CRC64;
MKLERPQVSL ASIAPLLPVL AVACALLAAW FGWSGWQQYQ DATRRDGVQQ SRDAVVQAIG
TTLAAERTRL EQQLENPVLR AAIGSGDFAR AGALLADGWP GASDGVVLAP ALDSAYAALP
EGGFGRLSVL EDALASDAPV AHVVDTAAGP KLALAAPVRL QEGGEVAAVA LVNLALERIT
GAVTNATLPG GTYLAVRQGG YNVVERGDAG LSGGAEVLAK PVTGAGLRVA AAVPDVAGGP
FGLAATGCLV AAAVLALLAA LALVAWRAPH LLTRRAGAQA EAEDGVPFPT LAEATDESPA
KTEQVPMSDA VAAPATNATA TGPVSIDRGI FRAYDIRGVV GRDLSPQVAE LIGQAIGSLM
QDKGLEDIVV GRDGRLSGPD MAGGLVTGLR KAGRNVIDIG LAPTPLVYFG AYQLQAGSCV
SVTGSHNPPD YNGFKIVVGG ETLSGDAITD LYARIADDRL HTAPSPGRLE QRTIDDDYIQ
RVASDIQIDR PLKVVVDAGN GVAGELGPKV LAAIGAEVVP LYCDIDGTFP NHHPDPSEPH
NLADLIQMVQ HLDADLGVAF DGDGDRLGVV TRDGHNIFPD RLLMLFAADV LERNPGAQII
FDVKCTGRLP GHVLRHGGSP LMWKTGHSLI KAKMRETGAE LAGEMSGHFF FGERWYGFDD
GIYSAARLLE ILAAQPGRPS DVLDALPDGV ATPEIKVDAP DGNPHAFVER FVANAAFADA
RLSTIDGLRV DWADGWGLVR ASNTTPVLVM RFDADNNEAM ARIKAAFREQ LLALRPDLDL
PF
//
