ID A0A0X1KPM4_9THEM Unreviewed; 477 AA.
AC A0A0X1KPM4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:AJC73203.1};
GN ORFNames=AJ81_02140 {ECO:0000313|EMBL:AJC73203.1};
OS Pseudothermotoga hypogea DSM 11164 = NBRC 106472.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=1123384 {ECO:0000313|EMBL:AJC73203.1, ECO:0000313|Proteomes:UP000077469};
RN [1] {ECO:0000313|EMBL:AJC73203.1, ECO:0000313|Proteomes:UP000077469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11164 {ECO:0000313|EMBL:AJC73203.1,
RC ECO:0000313|Proteomes:UP000077469};
RA Zhang X., Alvare G., Fristensky B., Chen L., Suen T., Chen Q., Ma K.;
RT "Genome sequencing of Thermotog hypogea.";
RL Submitted (JAN-2014) 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}.
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DR EMBL; CP007141; AJC73203.1; -; Genomic_DNA.
DR RefSeq; WP_031503653.1; NZ_JONI01000005.1.
DR AlphaFoldDB; A0A0X1KPM4; -.
DR STRING; 1123384.AJ81_02140; -.
DR PaxDb; 1123384-AJ81_02140; -.
DR KEGG; phy:AJ81_02140; -.
DR PATRIC; fig|1123384.7.peg.424; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000077469; 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; cd05799; PGM2; 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; 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 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000077469}.
FT DOMAIN 2..132
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 152..253
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 259..374
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 477 AA; 53488 MW; 5E41F003DC811DDE CRC64;
MILFGTGGVR GIMRDGEFDE KLIVDVSRAV ALWMYEEKLD GVVIAYDTRR NSNRFAKLAA
QTFADCGIET YLFDAPTPTP LLSFAVRELR VGAGVVITAS HNPPQYNGYK VYTSDGVQAV
PSHTEKISSL MGKSFRVNKT ARVQPVPKQV EERYIERLVR LVGKHVEGST KIVYSPLQGT
GARFVPKVLR ELGCDVICVE QQMEFDPNFS KVASLNPEDE RAFDMVRRVC QEEKARFGIA
TDPDCDRVGL IVDGKRLSGN QVGVLLTEML RHGANPESNL IKTIVTTDMV KPMCEELNLH
VLETPTGFKY IGHLIETKSK EPSFSYFLAF EESCGYLIGD LVRDKDGVLG SALIAGLCSK
YDPIELLNSL YERYGYHIEE LISMSFESPE QAKQKYEVLK LNPPTRIADQ EIVRIFDYEN
DPQMPNETLL FETGSVKIYV RPSGTEPKLK IYVKVVGYDE HEARSILGSV RKAVTEL
//
