ID M1X4U4_9NOST Unreviewed; 478 AA.
AC M1X4U4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase {ECO:0000313|EMBL:CCH66696.1};
GN ORFNames=RINTHH_5410 {ECO:0000313|EMBL:CCH66696.1};
OS Richelia intracellularis HH01.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Richelia.
OX NCBI_TaxID=1165094 {ECO:0000313|EMBL:CCH66696.1, ECO:0000313|Proteomes:UP000053051};
RN [1] {ECO:0000313|EMBL:CCH66696.1, ECO:0000313|Proteomes:UP000053051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH01 {ECO:0000313|EMBL:CCH66696.1,
RC ECO:0000313|Proteomes:UP000053051};
RA Hilton J.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH01 {ECO:0000313|Proteomes:UP000053051};
RA Hilton J.A., Foster R.A., Tripp H.J., Carter B.J., Zehr J.P.,
RA Villareal T.A.;
RT "Diatom-associated endosymboitic cyanobacterium lacks core nitrogen
RT metabolism enzymes.";
RL Submitted (JAN-2016) 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:CCH66696.1}.
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DR EMBL; CAIY01000027; CCH66696.1; -; Genomic_DNA.
DR RefSeq; WP_008232467.1; NZ_CAIY01000027.1.
DR AlphaFoldDB; M1X4U4; -.
DR STRING; 1165094.RINTHH_5410; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000053051; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05800; PGM_like2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053051}.
FT DOMAIN 8..144
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 162..267
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 277..380
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 424..467
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 478 AA; 52529 MW; EE7D34C71010BE9B CRC64;
MPVAANSIKF GTDGWRGVIA DEFTFERLAV VAPVAAKVLL NTYGEQVGNR KIVVGYDRRF
MAEDFAAKVS EAISAAGFDV LFSQTYAPTP AFSWAAKQEN ALGALVITAS HNPGKYSGLK
VKSAFGGSVP PEVTREIERS LNEEIPQAEE PGKIEYFNSW HNYCAELESK VDIAKIRSVI
ASGKLTLFAD VMHGAAAGGL ERLLGKGVKE INSNRDPTFE GGAPEPLPKY LSYFIQTMKN
YQHEQSTGLT VGLVFDGDCD RIAAVDGDAN FLSSQILIPI LIDHLTKRRN FSGEVVKTVS
GSDLIPRVAA LNNLSVFETP VGYKYITDRM LTAQVLLGGE ESGGIGYGNH IPERDALLSA
LYILEAVVES GLNLGEYYRQ LQLQTDFVSA YDRIDLPLAS MEVRARLLTQ LQTYPLNNIA
GKPVIDCQII DGYKFRLQDT SWLMIRFSGT EPVLRLYCEA PTLEQVHANL AWVKQWAE
//
