ID F8KXN6_PARAV Unreviewed; 459 AA.
AC F8KXN6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Phosphoglucosamine mutase {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327};
DE EC=5.4.2.10 {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327};
GN Name=glmM {ECO:0000256|HAMAP-Rule:MF_01554,
GN ECO:0000313|EMBL:CCB87533.1};
GN OrderedLocusNames=PUV_25830 {ECO:0000313|EMBL:CCB87533.1};
OS Parachlamydia acanthamoebae (strain UV7).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Parachlamydia.
OX NCBI_TaxID=765952 {ECO:0000313|EMBL:CCB87533.1, ECO:0000313|Proteomes:UP000000495};
RN [1] {ECO:0000313|EMBL:CCB87533.1, ECO:0000313|Proteomes:UP000000495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UV7 {ECO:0000313|Proteomes:UP000000495};
RX PubMed=21690563; DOI=10.1093/molbev/msr161;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S., Horn M.;
RT "Unity in variety--the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 28:3253-3270(2011).
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01554,
CC ECO:0000256|RuleBase:RU004327}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate;
CC Xref=Rhea:RHEA:23424, ChEBI:CHEBI:58516, ChEBI:CHEBI:58725;
CC EC=5.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01554,
CC ECO:0000256|RuleBase:RU004327};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01554};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01554};
CC -!- PTM: Activated by phosphorylation. {ECO:0000256|HAMAP-Rule:MF_01554}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|HAMAP-Rule:MF_01554,
CC ECO:0000256|RuleBase:RU004326}.
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DR EMBL; FR872580; CCB87533.1; -; Genomic_DNA.
DR RefSeq; WP_006342435.1; NC_015702.1.
DR AlphaFoldDB; F8KXN6; -.
DR STRING; 765952.PUV_25830; -.
DR KEGG; puv:PUV_25830; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_0_0; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000000495; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05802; GlmM; 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 HAMAP; MF_01554_B; GlmM_B; 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 InterPro; IPR006352; GlmM_bact.
DR NCBIfam; TIGR01455; glmM; 1.
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.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01554};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01554};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01554};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_01554}; Reference proteome {ECO:0000313|Proteomes:UP000000495}.
FT DOMAIN 9..143
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 165..261
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 266..378
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 383..451
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT ACT_SITE 107
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
SQ SEQUENCE 459 AA; 50295 MW; 0FE6CD80DD659016 CRC64;
MKDRTKSEKI FGTDGVRGKA NRSPMTVETA LALGRAAGKI FRSHEGKHRV VIGKDTRLSC
YMFENALISG LCSMGVDTLM VGPLPTPGVA FITRAYRADA GIVISASHNP YYDNGIKFFS
SDGFKLPDTW EKQMEELVST NNFDDSLPAD HDIGKNFKVT DADGRYIEFA KATFPRRLSL
KNLTIALDCA NGAGYKVAPL IFRELDAKVF VYGNNPDGLN INLQCGSLYP ETIQKAVIEH
RADVGIALDG DADRVIMVDE NAQIIDGDTI LAICAKDMQR RGILKGNKVV STIMSNFGFV
KAMEELGIEV IKSQVGDRYV IQDMLEHDAN LGGEQSGHLI FLDHNTTGDG LVCALQVMRI
MIETDSKLSD LAALVKKYPQ VCVNVKVSSK PTFEALPGVN QKVAEVEEIL GDSGRVLLRY
SGTENICRVM VEGPKLQQVQ QLANQIADEV RKQIGTPEK
//
