ID   A0A127MB67_9SPHN        Unreviewed;       469 AA.
AC   A0A127MB67;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:AMO70493.1};
GN   ORFNames=AZE99_00290 {ECO:0000313|EMBL:AMO70493.1};
OS   Sphingorhabdus sp. M41.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=1806885 {ECO:0000313|EMBL:AMO70493.1, ECO:0000313|Proteomes:UP000073959};
RN   [1] {ECO:0000313|EMBL:AMO70493.1, ECO:0000313|Proteomes:UP000073959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M41 {ECO:0000313|EMBL:AMO70493.1,
RC   ECO:0000313|Proteomes:UP000073959};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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; CP014545; AMO70493.1; -; Genomic_DNA.
DR   RefSeq; WP_067196843.1; NZ_CP014545.1.
DR   AlphaFoldDB; A0A127MB67; -.
DR   STRING; 1806885.AZE99_00290; -.
DR   KEGG; sphg:AZE99_00290; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000073959; 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; 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}.
FT   DOMAIN          14..124
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          158..259
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          263..371
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          379..456
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   469 AA;  50535 MW;  14F246726112C044 CRC64;
     MNAPKSHEFH STSLREYDIR GIIGETLGAD DAYAIGRGFG TLIARDGGTA VATGFDGRES
     SPMLEEALVR GLNDAGINAI SVGMGPTPML YYAESVLKTV QGGIMITGSH NPANYNGFKM
     VFQGRPFFGA DILGLGTMAA SGDWESGTGT LERIDIEDEY VERLLKNFTG GAFKIGWDCG
     NGAAGPVIEK LTRLLAERGA GEHHLLYTEV DGSFPNHHPD PTEEKNLADL KALVAEKGLD
     FGVAFDGDGD RIGAIDGMGR VIWGDQLLQI YAEDVLKSEP GATIIADVKA SQALYDRIAA
     LGGKPLMWKT GHSLIKSKMK ETGSPLAGEM SGHVFFKHDY YGFDDAPYAA IRLIQAATNI
     GKSVTQLRSD MVDMINTPEM RFQVDESRKF AVIDEILERL SASGADVNNT DGARVNTEDG
     WWLLRASNTQ DVLVARAEAK SQDGLDRLMA QIDEQLALSG LERGEQAGH
//