ID Q28MM8_JANSC Unreviewed; 543 AA.
AC Q28MM8;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN OrderedLocusNames=Jann_3117 {ECO:0000313|EMBL:ABD56034.1};
OS Jannaschia sp. (strain CCS1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=290400 {ECO:0000313|EMBL:ABD56034.1, ECO:0000313|Proteomes:UP000008326};
RN [1] {ECO:0000313|Proteomes:UP000008326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1 {ECO:0000313|Proteomes:UP000008326};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABD56034.1, ECO:0000313|Proteomes:UP000008326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1 {ECO:0000313|EMBL:ABD56034.1,
RC ECO:0000313|Proteomes:UP000008326};
RX PubMed=17526795; DOI=10.1128/AEM.02580-06;
RA Moran M.A., Belas R., Schell M.A., Gonzalez J.M., Sun F., Sun S.,
RA Binder B.J., Edmonds J., Ye W., Orcutt B., Howard E.C., Meile C.,
RA Palefsky W., Goesmann A., Ren Q., Paulsen I., Ulrich L.E., Thompson L.S.,
RA Saunders E., Buchan A.;
RT "Ecological genomics of marine Roseobacters.";
RL Appl. Environ. Microbiol. 73:4559-4569(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; CP000264; ABD56034.1; -; Genomic_DNA.
DR RefSeq; WP_011456238.1; NC_007802.1.
DR AlphaFoldDB; Q28MM8; -.
DR STRING; 290400.Jann_3117; -.
DR KEGG; jan:Jann_3117; -.
DR eggNOG; COG0033; Bacteria.
DR HOGENOM; CLU_009330_0_1_5; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000008326; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008326}.
FT DOMAIN 14..153
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 184..286
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 296..406
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 57090 MW; 17C402F96EFDCFDE CRC64;
MQPDTVATQP IAGQKPGTSG LRKKTRTFME PHFLENYVQS IIDGIGGVVG QTLVVGGDGR
YFNDRAIQVI LRMLAANGAA GAVVGQGGIL STPAASHLIR KRGTGGGFIL SASHNPGGID
ADFGLKFNGP NGGPASEGVT AKIFAATEAI TEYRIVEAQD VDLDTIGTST LGDLSVEIVN
PVADYAELME SLFDFGKIRA LFASGFRMRF DAMHAVTGPY ATAILEDTLG AATGTVINGT
PSPDFGQGHP DPNPVWAKTL MDEMYGDDSP DFGAASDGDG DRNMIVGRRQ YVTPSDSLAL
LAAHAHRAPA YANGLAGVAR SMPTSGAVDR VAEAQGIDCY ETPTGWKFFG TLLDAGKVTL
CGEESAGTGS DHVREKDGLW AVLLWLNILA DSGQSVADLM AALWRDFGRC YYSRHDYEDV
EVDKANAVMD GLRARLATLP GTQVAGLTVT FADEFAYDDP VDGSRAEAQG LRIGFEGGAR
AVFRLSGTGT VGATIRMYLE RLETSADALD QPAETALRPV VDAALTLSDL AALTGRDSPN
VIT
//
