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Database: UniProt
Entry: A0A1G8GPM8_9MICC
LinkDB: A0A1G8GPM8_9MICC
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ID   A0A1G8GPM8_9MICC        Unreviewed;       567 AA.
AC   A0A1G8GPM8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:SDH96293.1};
GN   ORFNames=SAMN04488693_104208 {ECO:0000313|EMBL:SDH96293.1};
OS   Arthrobacter subterraneus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=335973 {ECO:0000313|EMBL:SDH96293.1, ECO:0000313|Proteomes:UP000199258};
RN   [1] {ECO:0000313|EMBL:SDH96293.1, ECO:0000313|Proteomes:UP000199258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP_1H {ECO:0000313|EMBL:SDH96293.1,
RC   ECO:0000313|Proteomes:UP000199258};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNDT01000004; SDH96293.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8GPM8; -.
DR   STRING; 335973.SAMN04488693_104208; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000199258; Unassembled WGS sequence.
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; 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; 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   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:UP000199258}.
FT   DOMAIN          54..176
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          219..321
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          334..446
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          509..543
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   567 AA;  59812 MW;  D28B06084FBB3322 CRC64;
     MDLFTRAREW AAQDPDSETR AELEDLLTRA MNDDDAGQAA ALQQLEDAFS GPLVFGTAGL
     RAALGPGPNR MNRVVVRSAA AGLAAHALNL ADGAYAPRAV VGFDARRNSR IFAEETAAIF
     TAAGLQTFLM PSELPTPVLA YAVRALECEV GVMVTASHNP PEDNGYKVYL GGRAVEDNAR
     GVQIVAPHDA QIAEQIAAVT GVRLAESGWN VLPESIETDY VASVTALADG DAYPARDLSI
     VLTPLHGVGG RTAQQVLASA GFDTVQVVKE QAEPDAAFPT VEFPNPEEPG ALDLALAAAA
     DLDADLVLAN DPDADRMAAA AKDPATGEWR MLRGDETGAL LGLHLAARLG EDEKHDAVFA
     NSVVSSRLLG RIAEASGITH VQTLTGFKWI SRVPDLTYGY EEALGYCVAP NLVRDKDGLS
     AALLLAELAA ACKAEGKTLF DLLDELALVH GLHASDQLSV RVGSLGLLGA MMNRLREAPP
     SSFAGSDVVI AEDLAEGTSL PPTDGLLYVT RDDTRVIIRP SGTEPKLKCY LEVIEPVDSA
     AELTEAKTTA RTRLDAVIRD VEEALGL
//
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