ID A0A142MBC1_AMIAI Unreviewed; 506 AA.
AC A0A142MBC1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:MBB3705217.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:MBB3705217.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:MBB3705217.1};
GN ORFNames=FHS67_001529 {ECO:0000313|EMBL:MBB3705217.1};
OS Aminobacter aminovorans (Chelatobacter heintzii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Aminobacter.
OX NCBI_TaxID=83263 {ECO:0000313|EMBL:MBB3705217.1, ECO:0000313|Proteomes:UP000577697};
RN [1] {ECO:0000313|EMBL:MBB3705217.1, ECO:0000313|Proteomes:UP000577697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10368 {ECO:0000313|EMBL:MBB3705217.1,
RC ECO:0000313|Proteomes:UP000577697};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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:MBB3705217.1}.
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DR EMBL; JACICB010000005; MBB3705217.1; -; Genomic_DNA.
DR RefSeq; WP_067964407.1; NZ_JACICB010000005.1.
DR AlphaFoldDB; A0A142MBC1; -.
DR STRING; 83263.AA2016_4731; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000577697; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR43771; 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, ECO:0000313|EMBL:MBB3705217.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 44..165
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 190..279
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 285..396
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 430..494
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 506 AA; 54940 MW; 55EE761E4FC2D448 CRC64;
MNFKPVAQAS PNTFEFETLA LVKPTGFREY DARWWFGHPS SPKEPELNLI GVQALGMGIG
TLIRRLGAGP DIVVGHDFRS YSMSIKLALV AGLLAAGARV KDIGLALSPM AYFAQFALDT
PSVAMVTASH NENGWTGVKM GAQRPLTFGP DEMSALREIV LNGDFDLTDG GSYEFVPDFR
KTYIDDLVAG KRITRKLRVV AACGNGTAGA FAPEALERIG CEVIPLDIEL DHSFPRYNPN
PEDMQMLHAI RDKVLETGAD VGLGFDGDGD RCGVVDNEGN EIFADKVGVM LARDISALHP
NATFVVDVKS TGLFNTDTVL AANGAKTDYW KTGHSYLKRR VAELGAIAGF EKSGHFFFNP
PIGRGYDDGI VTAIAVCQML DRSPGKSMAD LYRDLPLTYG TPTMSPHCDD ELKYGVVDKV
VADFEAMKRN GDIFAGQKIV DLVTVNGVRV VAEDGTWGLV RASSNKPELV VVVESPVSSE
RRREMFEAVD AVLRRNPSVG AYNQTF
//
