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
//