ID A0A0B2BX49_9SPHN Unreviewed; 468 AA.
AC A0A0B2BX49;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:KHL24577.1};
GN ORFNames=PK98_11370 {ECO:0000313|EMBL:KHL24577.1};
OS Croceibacterium mercuriale.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceibacterium.
OX NCBI_TaxID=1572751 {ECO:0000313|EMBL:KHL24577.1, ECO:0000313|Proteomes:UP000030988};
RN [1] {ECO:0000313|EMBL:KHL24577.1, ECO:0000313|Proteomes:UP000030988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Coronado {ECO:0000313|EMBL:KHL24577.1,
RC ECO:0000313|Proteomes:UP000030988};
RA Coil D.A., Eisen J.A.;
RT "Draft genome sequence of Kirrobacter mercurialis.";
RL Submitted (NOV-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHL24577.1}.
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DR EMBL; JTDN01000002; KHL24577.1; -; Genomic_DNA.
DR RefSeq; WP_039097026.1; NZ_JTDN01000002.1.
DR AlphaFoldDB; A0A0B2BX49; -.
DR STRING; 1572751.PK98_11370; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000030988; Unassembled WGS sequence.
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; 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};
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:UP000030988}.
FT DOMAIN 10..138
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 154..257
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 261..368
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 377..455
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 468 AA; 50597 MW; 98A0E7C877316083 CRC64;
MSHQFHSTVL REYDIRGIIG ETLGADDARA IGRGFGTLLR RAGGKLVAVG YDGRVSSPML
EHALVEGLTA SGCDVRKVGM GPTPMLYYAE ASDEQVDGGI QITGSHNPAN YNGFKMVFKG
RPFFGEDIQT IGRMAAEGDW DDGTGEVHAL DVMDAYIERL LTGLEGVDPE QLGKLRIGWD
AGNGAAGPAL ELLAARLPGE HHLLFTEVDG NFPNHHPDPT VPENLNDLAK LVAEKNLDFG
VAFDGDGDRI GAIDGQGRII WGDQLLMIYA EDLLQRRPGV TIIADVKASR ALFDRVAELG
GKPLMWKTGH SLIKSKMKET GSPLAGEMSG HVFFADTYYG YDDALYAGIR LIAASARLGK
SVTELKSAMP AMLNTPEMRF QVDESRKFAA IQEVKDRLAG ATDVDVNDTD GVRVTNDDGW
WLLRASNTQD VLVARAESYT QEGLDKLMGQ IDEQLAASGL ERGPQAGH
//
