ID A0A0K9EVE9_9ACTO Unreviewed; 653 AA.
AC A0A0K9EVE9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Phosphomannomutase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACU19_00750 {ECO:0000313|EMBL:KMY24103.1};
OS Actinobaculum suis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=1657 {ECO:0000313|EMBL:KMY24103.1, ECO:0000313|Proteomes:UP000037036};
RN [1] {ECO:0000313|Proteomes:UP000037036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U311 {ECO:0000313|Proteomes:UP000037036};
RA Moreno L.Z., Amigo C.R., Gobbi D.S., Ferreira T.S., Santos A.P.,
RA Moreno A.M.;
RT "Draft genome sequences of Brazilian Actinobaculum suis isolated from urine
RT and preputial swab.";
RL Submitted (JUN-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}.
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:KMY24103.1}.
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DR EMBL; LFUS01000002; KMY24103.1; -; Genomic_DNA.
DR RefSeq; WP_049618825.1; NZ_LFUS01000002.1.
DR AlphaFoldDB; A0A0K9EVE9; -.
DR STRING; 1657.ACU20_00450; -.
DR PATRIC; fig|1657.3.peg.808; -.
DR Proteomes; UP000037036; 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; 4.
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 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 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 60..175
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 288..374
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 444..535
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 600..621
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 653 AA; 67746 MW; CA29FE9E7F0B0937 CRC64;
MPDGADITPD LVEVIARARE WALHDPDPVT RAELEAVLAR AETDAAAAQE LREAFAGPLH
FGTAGLRGRM GFGESRMNRA VVIRATAGLM AWLKERVREP IVVVGCDARH GSADFARAAV
QVISAAGGQA LALPERLPTP VTAYAVKKLG ADAGVMVTAS HNPAQDNGYK VYLGGRVAAG
PGAGVQIVPP VDTEIADLIA AAPPADEVAQ DRERVSAVDV VADYVAETAE LVRGTVSAGT
ASPGTAGASC ADSGIADVSA AGSGADGPHV AGAQTTNAAE NSTGADVPGA DLRIVLTPMH
GVGARVALEV LRASGFAHVH VVPEQVEPDP DFPTVAFPNP EEQGALDLAI ALAREESADI
VLALDPDADR CSAAVPWGST GQWRQLSGDE IGALLGNWIA SKTTPAAPAQ TAELVEQVAG
PGKQMAGPGT ALRAQTAELV SSRRVLANSI VSSRLLAEIA RKHGLDYAVT LTGFKWIARV
PDLLFGYEEA IGFCVNPGAV ADKDGVSACA LLARIAADLK AQGSSVQAYL DEIAREYGLY
ATAPLTFRVA DLSLISKGMQ QLRANPPRQL VGSPVTVFAD LAEGYGEVPP TDGILMLTEA
NDRVVVRPSG TEPKLKCYLE VVFAPSQEIP REEAAKRLNV LKRDVANACG FSL
//
