ID Q9ZD38_RICPR Unreviewed; 508 AA.
AC Q9ZD38;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE SubName: Full=PHOSPHOMANNOMUTASE (ExoC) {ECO:0000313|EMBL:CAA14961.1};
GN OrderedLocusNames=RP509 {ECO:0000313|EMBL:CAA14961.1};
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947 {ECO:0000313|EMBL:CAA14961.1, ECO:0000313|Proteomes:UP000002480};
RN [1] {ECO:0000313|EMBL:CAA14961.1, ECO:0000313|Proteomes:UP000002480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E {ECO:0000313|EMBL:CAA14961.1,
RC ECO:0000313|Proteomes:UP000002480};
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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; AJ235272; CAA14961.1; -; Genomic_DNA.
DR PIR; G71654; G71654.
DR RefSeq; NP_220885.1; NC_000963.1.
DR AlphaFoldDB; Q9ZD38; -.
DR SMR; Q9ZD38; -.
DR STRING; 272947.gene:17555589; -.
DR EnsemblBacteria; CAA14961; CAA14961; CAA14961.
DR KEGG; rpr:RP509; -.
DR PATRIC; fig|272947.5.peg.518; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_9_1_5; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000002480; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002480}.
FT DOMAIN 15..142
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 206..299
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 307..417
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 423..496
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 508 AA; 57085 MW; D15A4A63121EDA93 CRC64;
MTSNNIKGFM NINKEIFRAY DIRGNSIKHL TEEVAYKIGF CFANMSITKD NNKICVGLDG
RISSPTLCKA LELGLTDAGA EIINIGVVPT PVLYFADKHF MPSGSIMVTG SHNPRDDNGF
KMLQNGKSFF GTQIQTLLTR INGVRWLDHD LKSRCKMTIM SSWNEIKDQY TSDTLKFAGQ
LNSNSIQYIQ KGCYMSSIEF DVLKLYIKRI LEGININPKL KVAWDPGNGA TCNIIEELIK
HLTNKNIIIN SMIDGNFPNH HPDPTNPANL QELIKLVKEQ NCDIGIAFDG DGDRIGIISG
VGEILFGDQI LCIFAEDILK EHPNANIIVD VKASQFIVDK IKSFSGNTII CRTGHPFIKN
KMLETNALLA GEMSGHIFFA DKYFGFDDAI YAALRFLDLL SKSSKTLDKI IDELPKIYST
PEIKIFVTSR LKLQIIKEIK EKLLEAKIEF NDIDGVRVNT KNGWWLLRSS NTESIIVARA
ESVSKNGLKN IIAMMNKYLV EYDLLINY
//
