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Database: UniProt
Entry: A0A0M8KR24_9MICO
LinkDB: A0A0M8KR24_9MICO
Original site: A0A0M8KR24_9MICO 
ID   A0A0M8KR24_9MICO        Unreviewed;       600 AA.
AC   A0A0M8KR24;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:GAP79658.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:GAP79658.1};
GN   ORFNames=Y09_2509 {ECO:0000313|EMBL:GAP79658.1};
OS   Brachybacterium sp. SW0106-09.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=1704590 {ECO:0000313|EMBL:GAP79658.1, ECO:0000313|Proteomes:UP000037781};
RN   [1] {ECO:0000313|EMBL:GAP79658.1, ECO:0000313|Proteomes:UP000037781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SW0106-09 {ECO:0000313|EMBL:GAP79658.1,
RC   ECO:0000313|Proteomes:UP000037781};
RA   Qin Q.L., Li Y., Zhang Y.Z.;
RT   "Genome Sequencing of Brachybacterium sp. SW0106-09.";
RL   Submitted (SEP-2015) 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}.
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:GAP79658.1}.
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DR   EMBL; BCAK01000028; GAP79658.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8KR24; -.
DR   Proteomes; UP000037781; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:GAP79658.1};
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}.
FT   DOMAIN          84..207
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          251..349
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          362..464
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          532..565
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   600 AA;  62500 MW;  70144DB9837774B8 CRC64;
     MSPEPAAAPG PADDGTIAGE AGAAGPAGDA PGPDAELRAR VAAWIADDPD PVTRAALENL
     LEQADAGDAA AAEEIRDAFS GDLEFGTAGL RGRMAPGPRR MNLAVVSRAA RGLADHLTGD
     LGLEQPLVVI GFDARHRSED FARASAAIMT AAGCRVHLLE RHGPTPLIAF AVRHLGADAG
     IVVTASHNPP ADNGYKVYLG GRASAPDGQG VQIVPPSDAQ IAARIAAVGP VREIPRAAGW
     EVLGEQLRED YLAAICALPD PEGPRQVRIV HTAMHGVGTE TALAALHRTG FAEVHPVAKQ
     ADPDPDFPTV TFPNPEEPGA IDLALELART LEADVVIAND PDADRCAAAV LDPHLGDWRM
     LTGDELGVLL GDHLIRRHGY AGTVANSVVS SRWLGRIAQA AGLEAATTLT GFKWIARAPG
     IVFGYEEAIG YCVLPEVVRD KDGLSAALMV AEMAALARAE GTTLVGRLDE LAREHGLFAT
     SQLSLRVTEL AERDVMMARL RAEPPAALAG SEVSDVQDLA EGSAETTGLP ATDGVLLATA
     DDARVIVRPS GTEPKLKCYI EVREEVPAGA DEAALGEVRR AASAHLEQIT EEMRTALTGA
//
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