ID A0A099U7V8_9HELI Unreviewed; 446 AA.
AC A0A099U7V8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Phosphoglucosamine mutase {ECO:0000256|HAMAP-Rule:MF_01554};
DE EC=5.4.2.10 {ECO:0000256|HAMAP-Rule:MF_01554};
GN Name=glmM {ECO:0000256|HAMAP-Rule:MF_01554};
GN ORFNames=CDV25_03145 {ECO:0000313|EMBL:AWI33868.1}, LS72_008290
GN {ECO:0000313|EMBL:TLE14841.1};
OS Helicobacter apodemus.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=135569 {ECO:0000313|EMBL:TLE14841.1, ECO:0000313|Proteomes:UP000029920};
RN [1] {ECO:0000313|EMBL:TLE14841.1, ECO:0000313|Proteomes:UP000029920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT-03-7007 {ECO:0000313|EMBL:TLE14841.1,
RC ECO:0000313|Proteomes:UP000029920};
RX PubMed=25428971;
RA Sheh A., Shen Z., Fox J.G.;
RT "Draft genome sequences of eight enterohepatic helicobacter species
RT isolated from both laboratory and wild rodents.";
RL Genome Announc. 2:e01218-e01214(2014).
RN [2] {ECO:0000313|EMBL:AWI33868.1, ECO:0000313|Proteomes:UP000244890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCJK1 {ECO:0000313|EMBL:AWI33868.1}, and SNUVETPUB-15-01
RC {ECO:0000313|Proteomes:UP000244890};
RA Cho S.;
RT "Complete genome of Helicobacter apodemus.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:TLE14841.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MIT-03-7007 {ECO:0000313|EMBL:TLE14841.1};
RA Sheh A., Shen Z., Mannion A.J., Fox J.G.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01554}.
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 -!- 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}.
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DR EMBL; CP021886; AWI33868.1; -; Genomic_DNA.
DR EMBL; JRPC02000022; TLE14841.1; -; Genomic_DNA.
DR RefSeq; WP_034554954.1; NZ_JRPC02000022.1.
DR AlphaFoldDB; A0A099U7V8; -.
DR GeneID; 82133191; -.
DR KEGG; had:CDV25_03145; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000029920; Unassembled WGS sequence.
DR Proteomes; UP000244890; 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; 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.
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:UP000029920}.
FT DOMAIN 3..134
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 158..255
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 259..370
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 405..435
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT ACT_SITE 99
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 99
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 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
SQ SEQUENCE 446 AA; 49173 MW; 4D784A747DFC2B06 CRC64;
MDLFGTDGVR GVAGAKLNVF CALKLGIAAG IYYRKHSKTN KILVGKDTRR SGYMLENALV
SGLTSVGYEV IQIGPMPTPA IAYLTEDMRC DGGIMVSASH NLYADNGIKF FGKSGYKLDE
KDEKNIEKIY ADEDLLESSQ KRGKEIGSSK RIDDVVGRYI VHIKNSFPKD LSLHGVRIVI
DCANGAAYKV APTIFNELGA EVFVINDTPN GFNINESCGA TQPLSLQEEV RKVRADIGFA
LDGDADRLVV VDEKGNVVNG DKLIGVLALA VKENQTLKHN TIVATIMSNY ALEEFLGEHN
IKLIRSNVGD KYVLESMLEH HLNFGAEQSG HIIFSDFAKT GDGLVSALQT MAYILRFNKP
ASEILDCFEL YPQILKNLPI DSKPNLEGLE GYGTFLKGIA SKKIRHLIRY SGTENKLRIL
LEGKDLKLLE NTMQECEAYF KGKIYS
//
