ID A0Y9M0_9GAMM Unreviewed; 836 AA.
AC A0Y9M0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=GP2143_16251 {ECO:0000313|EMBL:EAW32824.1};
OS marine gamma proteobacterium HTCC2143.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; BD1-7 clade.
OX NCBI_TaxID=247633 {ECO:0000313|EMBL:EAW32824.1, ECO:0000313|Proteomes:UP000004931};
RN [1] {ECO:0000313|EMBL:EAW32824.1, ECO:0000313|Proteomes:UP000004931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2143 {ECO:0000313|EMBL:EAW32824.1,
RC ECO:0000313|Proteomes:UP000004931};
RX PubMed=20601481; DOI=10.1128/JB.00683-10;
RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of the oligotrophic marine Gammaproteobacterium HTCC2143,
RT isolated from the Oregon Coast.";
RL J. Bacteriol. 192:4530-4531(2010).
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:EAW32824.1}.
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DR EMBL; AAVT01000001; EAW32824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0Y9M0; -.
DR STRING; 247633.GP2143_16251; -.
DR eggNOG; COG1109; Bacteria.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000004931; 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:UP000004931};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 386..516
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 531..628
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 633..738
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 774..825
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 90956 MW; 5D14018CACA4866E CRC64;
MANKKTRNNK PGETSKSNAK PENKLRSTLS NSAILSLLIV GIMFVYIALV ERPAINNATV
QAQAQSLADS QASLIDQALS QLQLRLSNIA ISPELLTGLD VQDSQMVNRY RQELARAFPE
AIDTKLIALG PLGIASRDKK NWALRNNIEL DLLRYASNGR PVEPEAYKID GKWLFSLATP
IKALNKAYAS GALLVTLDES YLLTLLGQLD SSLGQSQLIQ QFQNKQHIIA SRGDAGDASL
AATADTSISH WQINFTPSKE MIAQSRNTAS MVWIMLAVAI TALILSALSA HSTLKKALAW
NLEKLTTTKK STTVGYTLPG FEEVAQRLKE VPTITVKSKE PEPEMLVDLV DPLMDIINSG
PLTLDELTND KPAENVVLPN QLPDSIFRAY DIRGLAESEL TDQTVFAIAM AIGSEALDNG
QQSIIVAADG RHSSPRIRKA MIAGLQASGT DVIDIGAQPT PLMYFATHQL NTQSGVMITG
SHNPAEYNGI KIVIGGKALS GDAIQSLKER ILNNDFANGS GDYQTQLIDQ AYIDFIINDV
AIAQPLKIVI DAGNGITGAI APRLFEELGC EVIPLYCEVD GDFPNHHPDP TVEANLKDLK
RAVSDNAADL GIAFDGDGDR LGVVTASGKS VPADRLLMLL AQDVVSRNPG ADVIFDVKCS
RNLNTLISNY GGRPIMWKSG HSFMKEKMVE TGALLGGEFS GHIFFKERWF GFDDGMYAAA
RLVEILSTTD PDLDLQLEAF PDSIGSPELK IESTESQKFI VIEQLINTAN FGEGKRSTLD
GLRVDFPDGW GLVRASNTTP MLVLRFEADT EQAMEHIQNL FKEQLSLVDD SLCFNF
//
