ID M2Y9F3_9NOCA Unreviewed; 455 AA.
AC M2Y9F3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:EME51552.1};
GN Name=manB {ECO:0000313|EMBL:EME51552.1};
GN ORFNames=G352_25222 {ECO:0000313|EMBL:EME51552.1};
OS Rhodococcus ruber BKS 20-38.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1278076 {ECO:0000313|EMBL:EME51552.1, ECO:0000313|Proteomes:UP000011731};
RN [1] {ECO:0000313|EMBL:EME51552.1, ECO:0000313|Proteomes:UP000011731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BKS 20-38 {ECO:0000313|EMBL:EME51552.1,
RC ECO:0000313|Proteomes:UP000011731};
RX PubMed=23558535;
RA Bala M., Kumar S., Raghava G.P., Mayilraj S.;
RT "Draft Genome Sequence of Rhodococcus ruber Strain BKS 20-38.";
RL Genome Announc. 1:E0013913-E0013913(2013).
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:EME51552.1}.
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DR EMBL; AOEX01000100; EME51552.1; -; Genomic_DNA.
DR RefSeq; WP_003939104.1; NZ_AOEX01000100.1.
DR AlphaFoldDB; M2Y9F3; -.
DR PATRIC; fig|1278076.4.peg.5169; -.
DR Proteomes; UP000011731; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03089; PMM_PGM; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 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.
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 12..128
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 159..258
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 266..372
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 377..453
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 455 AA; 47992 MW; CEC3919643333C2D CRC64;
MARTAESVSA VVKAYDVRGL VGEQLDAGFV RDVGASFARL MRDGGATRVV IGHDMRASSP
ELAEAFAAGV TAQGVDVVHI GLASTDQLYF ASGILEAPGA MFTASHNPAR YNGIKLCRAG
AKPVGQETGL ATVAAELVAG VPDFDGAPGT VTERDVLADY AAFVRSLVDL SAMRPLRVAV
DAGNGMGGHT VPAVFGALPI DLVPLYFELD GTFPNHEANP LDPANLVDLQ KLVRDSGADL
GLAFDGDADR CFVVDERGEP VTPSAVTALV ASRELAKEPG STIIHNLITS RAVPELVTEL
GGKPVRTRVG HSFIKQQMAE TGAVFGGEHS AHYYFRDFWG ADSGMLAALH VLAALAGQDR
PLSELMREYD RYAASGEINS TVDDAAERTA AVLEAFGDRA EAVDRLDGVT VDLADGAWFN
LRASNTEPLL RLNVEARTAE QVDALVREIL AIVRA
//
