ID A0A073CL73_PLAAG Unreviewed; 843 AA.
AC A0A073CL73;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Mpg3 {ECO:0000313|EMBL:KEI68682.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:KEI68682.1};
GN Name=mpg3 {ECO:0000313|EMBL:KEI68682.1};
GN ORFNames=A19Y_3959 {ECO:0000313|EMBL:KEI68682.1};
OS Planktothrix agardhii NIVA-CYA 126/8.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI68682.1, ECO:0000313|Proteomes:UP000027395};
RN [1] {ECO:0000313|EMBL:KEI68682.1, ECO:0000313|Proteomes:UP000027395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI68682.1,
RC ECO:0000313|Proteomes:UP000027395};
RX PubMed=24907328; DOI=10.1128/AEM.01188-14;
RA Christiansen G., Goesmann A., Kurmayer R.;
RT "Elucidation of insertion elements encoded on plasmids and in vitro
RT construction of shuttle vectors from the toxic cyanobacterium
RT Planktothrix.";
RL Appl. Environ. Microbiol. 80:4887-4897(2014).
RN [2] {ECO:0000313|EMBL:AQY60435.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:AQY60435.1};
RX PubMed=28261178; DOI=10.3389/fmicb.2017.00219;
RA Entfellner E., Frei M., Christiansen G., Deng L., Blom J., Kurmayer R.;
RT "Evolution of Anabaenopeptin Peptide Structural Variability in the
RT Cyanobacterium Planktothrix.";
RL Front. Microbiol. 8:219-219(2017).
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; KU665237; AQY60435.1; -; Genomic_DNA.
DR EMBL; CM002803; KEI68682.1; -; Genomic_DNA.
DR RefSeq; WP_042156138.1; NZ_CM002803.1.
DR AlphaFoldDB; A0A073CL73; -.
DR STRING; 388467.A19Y_3959; -.
DR PATRIC; fig|388467.6.peg.3900; -.
DR eggNOG; COG1109; Bacteria.
DR eggNOG; COG1208; Bacteria.
DR HOGENOM; CLU_017652_1_0_3; -.
DR Proteomes; UP000027395; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProt.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0043886; F:structural constituent of carboxysome shell; IEA:UniProt.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05805; MPG1_transferase; 1.
DR CDD; cd04181; NTP_transferase; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 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; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR22572:SF15; MANNOSE-1-PHOSPHATE GUANYLTRANSFERASE BETA; 1.
DR PANTHER; PTHR22572; SUGAR-1-PHOSPHATE GUANYL TRANSFERASE; 1.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Isomerase {ECO:0000313|EMBL:KEI68682.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000027395};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..231
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 383..513
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 534..631
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 639..744
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 843 AA; 93087 MW; C50B9A745208DFC7 CRC64;
MRAVLMAGGS GTRLRPLTCD LPKPMVPILN RPIAEHIINL LKQHNITEVI ATLHYLPDVM
REYFHDGSHL GVQITYAVEE DQPLGTAGCV KNIAELLDKT FLVISGDSVT DFDLTAAIEF
HQQKQSKATL ILTRMPNPIE FGVVITDENY RINRFLEKPA ASEVFSDTVN TGTYILEPEV
LEYLPFDQEC DFSQDLFPLL LEKGIPMYGF IANNYWCDIG HLDIYREAHY DALMGKVKLK
IAYPEPSPGL WIGENTFIDE TAVIETPVLI GRNCRIGARA QIEAGSVIGD NITIGADANI
KRPIIWNGAI IGDDAHLRAC VIARGARVGR RAHVLEGAVV GSLSSVGEEA QISPGVRVWP
SKKIESGATL NINLIWGNTA QRNLFGQRGV QGLANIDITP EFAVKLGAAF GSTLKPGSLV
AVSRDQRPIS RMVTRSLVAG LMSVGVNIIN LDATAIPITR TAIPTLNVAG GIHVRLSPER
ADYLLIEFLD NKGISITKAK EKKIEGAYFK EDLRRAQIPE IGNVSYTVDL LDIYSASFSK
HINSEILRYS NAKVVIDYVY AVSGAILPQL LAKFGCDAVV LNASLNHTAL SVPERENLLD
QLGRVVEALR ANFGAQVYAN GEQFMLVDET GSPIRGEFLT SLMVNMVLTS HPRSTIVVPV
HTSSAVEQIA RRYDAKVIRT KANPTALMEA CHRNPNVVLG GSGDMGFIFP QLHPGFDAMF
SIAKIIELLT SQERSLTQVR ADLPHVVHRR YTVRCPWTIK GALMRHLVET HSPDNLELID
GVKLINYQDD NWVLVLPDAG EPQVHIFANS VDRDWVDTTL REYRNLVHDF VNQSQGMDHR
EDI
//
