ID A0A0A1YMF0_9PSED Unreviewed; 854 AA.
AC A0A0A1YMF0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=TMS3_0103735 {ECO:0000313|EMBL:KFX71070.1};
OS Pseudomonas taeanensis MS-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1395571 {ECO:0000313|EMBL:KFX71070.1, ECO:0000313|Proteomes:UP000030063};
RN [1] {ECO:0000313|EMBL:KFX71070.1, ECO:0000313|Proteomes:UP000030063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS-3 {ECO:0000313|EMBL:KFX71070.1,
RC ECO:0000313|Proteomes:UP000030063};
RX PubMed=24407626;
RA Lee S.Y., Kim S.H., Lee D.G., Shin S., Yun S.H., Choi C.W., Chung Y.H.,
RA Choi J.S., Kahng H.Y., Kim S.I.;
RT "Draft Genome Sequence of Petroleum Oil-Degrading Marine Bacterium
RT Pseudomonas taeanensis Strain MS-3, Isolated from a Crude Oil-Contaminated
RT Seashore.";
RL Genome Announc. 2:0-0(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}.
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:KFX71070.1}.
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DR EMBL; AWSQ01000001; KFX71070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1YMF0; -.
DR STRING; 1395571.TMS3_0103735; -.
DR eggNOG; COG1109; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000030063; 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: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:UP000030063};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 404..534
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 549..646
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 651..757
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 766..843
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 334..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 91930 MW; C18054353EF95A86 CRC64;
MKGFKRTAKD AAPGPKKPEA KTWLPGLLAA GAGLALAAGL LWFAVFDGIH QQQQAQLSQA
WGGGQAAALQ QALKQLAADT QAAAHNPQLL EALQSQETEA IHSAERNLSY WHGVVDAHLN
APGQAVQDMN RRAPMNFAAL DMLRRVEKGQ TPAVEAYKID QRWLVYSAAP VRLSDDQPQQ
GTLLLAVELE RLLASIPPLP AEVGQVQLLQ QFGNTTPQLL TQRGQAQGAA QRFSSGNPHW
TLSFTPGPAL TEAAFSLPLL GLVLSLALAG VLLGLYLVHS GLQRRLRDDV RQLGQLLNEL
STGKSVKVFS LGLPALDSLA QALARLPRRA YATATNASAD TPRSDAGQAT AAAPSEPADL
VDPLFQDADI LDIDFLDEDQ DLLGLEQTPV MNTPHLAPKL PADIFRAYDI RGVVGTSLTA
ETAYWVGRAI GSQSLAQGEP NVAVGRDGRL SGPELVQHLI QGLLDCGCTV SDVGMVPTPV
VYYAANILSG KSAVMLTGSH NPPDYNGFKI VIAGDTLANE QIQALKTRID NNDLASGVGT
VEQVDVLERY FKQIRDDIAL AKPLKVVVDC GNGAAGVIAP QLIEALGCTV IPLFCDVDGN
FPNHHPDPGK PENLVDLIAK VKAEKADLGL AFDGDGDRVG VVTNTGTMVY PDRLLMLFAK
DVVSRNPGAD IIFDVKCTRR LTPLISGYGG RPVMWKTGHS LIKKKMRETG ALLAGEMSGH
IFFKERWFGF DDGIYAAARL LEILSQDKRD AEQVFAAFPS DISTPEINIQ VTEQSKFSII
DALQRNGAWG EANITTLDGV RVDYPKGWGL VRASNTTPVL VLRFEAESDE ELERIKQVFR
TQLHGVAPDL NLPF
//
