ID A0A2S5R9I7_9PROT Unreviewed; 458 AA.
AC A0A2S5R9I7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 02-APR-2025, entry version 20.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:PPE03984.1};
GN ORFNames=HCUR_00519 {ECO:0000313|EMBL:PPE03984.1};
OS Holospora curviuscula.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Holosporales; Holosporaceae; Holospora.
OX NCBI_TaxID=1082868 {ECO:0000313|EMBL:PPE03984.1, ECO:0000313|Proteomes:UP000239425};
RN [1] {ECO:0000313|EMBL:PPE03984.1, ECO:0000313|Proteomes:UP000239425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=02AZ16 {ECO:0000313|Proteomes:UP000239425};
RA Garushyants S.K., Beliavskaya A., Malko D.B., Logacheva M.D., Rautian M.S.,
RA Gelfand M.S.;
RT "Comparative genomic analysis of Holospora spp., intranuclear symbionts of
RT paramecia.";
RL Submitted (NOV-2017) 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}.
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:PPE03984.1}.
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DR EMBL; PHHC01000079; PPE03984.1; -; Genomic_DNA.
DR RefSeq; WP_104206607.1; NZ_PHHC01000079.1.
DR AlphaFoldDB; A0A2S5R9I7; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000239425; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:TreeGrafter.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:TreeGrafter.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:TreeGrafter.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:TreeGrafter.
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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR050060; Phosphoglucosamine_mutase.
DR PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000239425}.
FT DOMAIN 6..149
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 184..265
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 270..354
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 408..432
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 458 AA; 50706 MW; 9E7077490A3E98A2 CRC64;
MQKLRWFGTD GIRGVAFEGL FVPSILTRIG CAFADYLHKK LSKNFGKKSR KDSQKSLWVL
MGMDTRDSGS EFLFALAAGL EEGRVGIGNL GVCSSGALAW LTRYYGADFG IMVSASHNTS
LYNGIKFFDS KGSKLSSEEE LEIEFFIDQY IQDSKKTVRK YFNKHVSYSQ LPYTQALIQD
RDLMGLRVVL DGAHGSLWNF AAQCFKACGA HVLATLGSAP NGHNINENIG VLYPNHLQQA
VLAHSADLGF CFDGDGDRVG VVDALGKYWN GDHILAVLAQ EAMSMVGTVM SNYGLERHCR
ENGRSFFRVD VGDRWIAQAL KAYGLRWGGE ASGHIIDHSF LPVGDGLWIA LELSTKFLKG
MKAPLFPAFT PYPVMQCALP ITENFSFLES DTQSYLHTLR ASLEPHIRLV IRPSGTEPVI
RVLVEGPCSV ELKCVMEHVL GWLSRYTKAE KIFESSVA
//
