ID A3D2W2_SHEB5 Unreviewed; 573 AA.
AC A3D2W2;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I {ECO:0000313|EMBL:ABN61075.1};
GN OrderedLocusNames=Sbal_1561 {ECO:0000313|EMBL:ABN61075.1};
OS Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=325240 {ECO:0000313|EMBL:ABN61075.1, ECO:0000313|Proteomes:UP000001557};
RN [1] {ECO:0000313|EMBL:ABN61075.1, ECO:0000313|Proteomes:UP000001557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS155 / ATCC BAA-1091 {ECO:0000313|Proteomes:UP000001557};
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., Dalin E., Tice H., Pitluck S.,
RA Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS155.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000563; ABN61075.1; -; Genomic_DNA.
DR RefSeq; WP_011846431.1; NC_009052.1.
DR AlphaFoldDB; A3D2W2; -.
DR STRING; 325240.Sbal_1561; -.
DR KEGG; sbl:Sbal_1561; -.
DR HOGENOM; CLU_016950_0_0_6; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000001557; 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 45..185
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 213..314
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 326..444
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 489..540
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 573 AA; 62344 MW; 6F7076C9766AD091 CRC64;
MNTHLQLQVN HWLENDPDPR TQTQLQTLID NGSEAELAAR FAGRLEFGTA GLRGVVGAGP
MGMNRLVIRQ TSAGLGAYLL DQIKDAAERG VVIGYDGRHD SFNFAHDAAS VLTAMGIKVR
LTSKVAPTPL VAFGVKHFNA AAGIVVTASH NPPQYNGYKV YWENGAQIIP PHDSGIAAQI
ERAANQAIPF LEHDEAVKQG KLTLLQDDFY QSYRHGVQHA EVLQNHTAPE KVSLAYTAMH
GVGAEMAETV LKDAGFTQVY SVASQREPDG DFPTVNFPNP EEKGAMDLVI AEAKKHGAML
ACANDPDADR FAVAVRRDDG EYQMLTGDQV GVLFGHYLLS HAKDNQRLTG TTIVSSSLLS
KIAQGFGTQS FTTLTGFKWL MNVGIAKTSP EDQFLFAYEE ALGYTVGSMV WDKDGLSALV
AFAQLTAELV AKGQTIWDRL EQIYREHGFH LNAQVSIALK PDTPNIGAYL REHPPVKIGE
HDVLSTDDLK ALERRFADGS VEKIDLPPSD VLTYCLAGGA RVIVRPSGTE PKIKCYYEVV
ETMVDTDTLA SAQARASKAM DDFIQAHQAS LPK
//
