ID A0A2N6PER9_9MICO Unreviewed; 599 AA.
AC A0A2N6PER9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:PMB97177.1};
GN ORFNames=CJ198_12785 {ECO:0000313|EMBL:PMB97177.1};
OS Brevibacterium luteolum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=199591 {ECO:0000313|EMBL:PMB97177.1, ECO:0000313|Proteomes:UP000235703};
RN [1] {ECO:0000313|EMBL:PMB97177.1, ECO:0000313|Proteomes:UP000235703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0680 {ECO:0000313|EMBL:PMB97177.1,
RC ECO:0000313|Proteomes:UP000235703};
RA Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT "Bacterial strain isolated from the female urinary microbiota.";
RL Submitted (SEP-2017) 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:PMB97177.1}.
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DR EMBL; PNFZ01000009; PMB97177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6PER9; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000235703; 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:UP000235703}.
FT DOMAIN 72..187
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 254..355
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 375..469
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 535..585
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 61989 MW; 6DA774B72F4C7A21 CRC64;
MSPAQPPQSQ PPQPPAPTVF TDGFDADIVK SWIADDPDEQ TRTELAALLE SATAGDAAAI
AELEDRFAAP LTFGTAGLRG ALGGGPNRMN RAVVIRAAAG LAGFLRDTLG EGFRVVIGCD
ARHGSADFAR DTAAVVTAAG GQALLLPDKL PTPVLAFALG HLDCDAGVMV TASHNPPQDN
GYKVYLGARP LQAVLDRQGD AQAAAAAEAG AGAQIVPPFD DLIAAHIAGI ATVADTPRAE
SGWKTVSEQI VEDYLASIDA LGQRLGAVRT APVRIVITSL HGVGGATMRA ALERAGFDDV
HAVASQEQPD PDFPTVTFPN PEEDGALDAA IALADAVGAD LIIANDPDAD RMSAAVPVHP
AAGAEEGTSG WRQLTGDEVG LLLGEHIAAR SPQDAVLANS IVSSRALAAA AKSHGLEHAA
TLTGFKWISR VPGAAFGYEE ALGYCVDPDV VRDKDGISAG VVFASLVSAL AEQARNVDGE
LKRIRTRDGA FVTQPLTFRL TDTSLIGEAM ARLRAAAPEQ LAGHDVTEVI DLAEGSGQLP
PTDGIMLLTA AGDRVIIRPS GTEPKLKCYL EAVGAVEEIE AARARLEQMR ADLTLFFGL
//
