ID A0A1Y1CN07_9BACT Unreviewed; 581 AA.
AC A0A1Y1CN07;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:BAX81352.1};
GN ORFNames=ALGA_3052 {ECO:0000313|EMBL:BAX81352.1};
OS Labilibaculum antarcticum.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Labilibaculum.
OX NCBI_TaxID=1717717 {ECO:0000313|EMBL:BAX81352.1, ECO:0000313|Proteomes:UP000218267};
RN [1] {ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT from the Antarctic marine sediment.";
RL Mar. Genomics 0:0-0(2017).
RN [2] {ECO:0000313|EMBL:BAX81352.1, ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|EMBL:BAX81352.1,
RC ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT from the Antarctic marine sediment.";
RL Mar. Genomics 39:1-2(2018).
RN [3] {ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Labilibaculum antarcticum sp. nov., a novel facultative anaerobic,
RT psychrotorelant bacterium isolated from marine sediment of Antarctica.";
RL Antonie Van Leeuwenhoek 113:349-355(2020).
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; AP018042; BAX81352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1CN07; -.
DR KEGG; mbas:ALGA_3052; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000218267; Chromosome.
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; cd05799; PGM2; 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; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 51..189
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 215..317
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 327..451
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 516..559
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 581 AA; 65419 MW; DE12D4F527DFB20B CRC64;
MNETEIFKIV NEKAQAWLEG KYDQETKNAV KSLLEKEDKT DLIESFYKDL EFGTGGLRGK
MGPGTNRMNI YTVGAATQGL ANYINKAFAG QENLSVCIGY DCRNNSKLYS DTVANIFSAN
GIKAYIFEDL RPTPEMSFAI RHLGCQSGVI ITASHNPKEY NGYKAYWEDG SQLVIPHDKN
VIDEVKAVKL EEIKFKGNPA LIEVLGEDMD KLFLDKVKTL SLSPEAIKNQ KDLKIVFTPL
HGTTVRLVPA SLKNYGFENV IHIPEQDVVD GNFPTVWSAN PEEPEALKMA VDKAKEVNAD
IVMACDPDGD RLGIAATNDK GEWEIVNGNQ TALIFNYYLI RRRKELGLLT GNDYVVKTIV
TTELFKEVAE KNNVQCFDAY TGFKWIAYVI RKNPEKNYIG GGEESFGYMP GDFTRDKDAV
SSCSIMAEIA AWAKEQGKNV FDILKDIYVE YGYSKEKMIY IVREGLQGAQ EIEKLMYDYR
YNRPKEINGS TLVLVKDYTT RIATNPVTGE ETALNFETTA DVLQFYLEDG TKISVRPSGT
EPKIKYYFEV RETLASIEDF YATEEKANKK IQGIISSLKL N
//
