ID G2IR86_SPHSK Unreviewed; 460 AA.
AC G2IR86;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase {ECO:0000313|EMBL:BAK68452.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:BAK68452.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:BAK68452.1};
GN ORFNames=SLG_37770 {ECO:0000313|EMBL:BAK68452.1};
OS Sphingobium sp. (strain NBRC 103272 / SYK-6).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=627192 {ECO:0000313|EMBL:BAK68452.1, ECO:0000313|Proteomes:UP000001275};
RN [1] {ECO:0000313|EMBL:BAK68452.1, ECO:0000313|Proteomes:UP000001275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103272 / SYK-6 {ECO:0000313|Proteomes:UP000001275};
RX PubMed=22207743; DOI=10.1128/JB.06254-11;
RA Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S.,
RA Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., Katano Y.,
RA Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., Fukuda M.,
RA Yamazaki S., Fujita N.;
RT "Complete genome sequence of Sphingobium sp. strain SYK-6, a degrader of
RT lignin-derived biaryls and monoaryls.";
RL J. Bacteriol. 194:534-535(2012).
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; AP012222; BAK68452.1; -; Genomic_DNA.
DR RefSeq; WP_014078091.1; NC_015976.1.
DR AlphaFoldDB; G2IR86; -.
DR STRING; 627192.SLG_37770; -.
DR KEGG; ssy:SLG_37770; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_9_1_5; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000001275; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:BAK68452.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001275}.
FT DOMAIN 10..127
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 157..250
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 254..362
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 370..447
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 460 AA; 49541 MW; 4E672467BAF621FA CRC64;
MPHQFHPTTL REYDIRGIIG ETLGEGDAYA IGRGFGTRVA RAGGSRVAVG YDGRLSSPAL
EEALVRGLNE SGIHVLRIGL GPTPMLYYAE AVLDVDGGIQ ITGSHNPANY NGFKMVLHHG
PFFGPDIQSL GTMAASGDWV DGSAGSETVE IADRYAARLV EGFEGKAFRI GWDAGNGAAG
PIVEKLVRLL PGEHYTLFTE VDGTFPNHHP DPTEEKNLTD LRTLVAEKAL DFGVAFDGDG
DRIGAIDGEG RIIWGDQLLA IFAEPVLRAV PGATIIADVK ASQALFDRVA QLGGTPLMWK
TGHSLIKSKM RETGSPLAGE MSGHIFFKHE YYGFDDALYA AVRLIRAASD LGKSVTELRG
EMPPMVNTPE LRFQVDESRK FAVIDEVLAR LRESGAQVDA TDGARVNTPD GWWLLRASNT
QDVLVARAEA RDEAGLDRLM AQIDEQLALS GLQRGAQAGH
//
