ID   EXOC_AZOBR              Reviewed;         469 AA.
AC   P45632;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Phosphomannomutase;
DE            Short=PMM;
DE            EC=5.4.2.8;
GN   Name=exoC;
OS   Azospirillum brasilense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RA   Petersen D.J., Vanderleyden J.;
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC         Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC         EC=5.4.2.8;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; U20583; AAA63608.1; -; Genomic_DNA.
DR   AlphaFoldDB; P45632; -.
DR   SMR; P45632; -.
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; 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; IPR016066; A-D-PHexomutase_CS.
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.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Isomerase; Magnesium; Metal-binding; Phosphoprotein.
FT   CHAIN           1..469
FT                   /note="Phosphomannomutase"
FT                   /id="PRO_0000147832"
FT   ACT_SITE        106
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   469 AA;  51130 MW;  82A7D10244BD9FEF CRC64;
     MSEAHTFHPT VLREYDIRGI VGSTLTAADA RAVGRLRHRG RPAAVRKTVC VGYDGRLSSP
     ELEAAMVDGL VACGLHVLRI GLGPTPMLYF ATRDREAAAG IMITGSHNPP DYNGIKMMLG
     KGPVYGRQIL DIGAIASKAD YVSGEGSSEQ LDIKDAYVER LLRDDDGTRD LTIAWDAGNG
     ASGEDPAPPD REVPGKHVLL FDEIDGNFPN HHPDPTVEKN LVDLKAAVAE HGCDIGIGFD
     GDGDRIGAID HLGRVVWGDQ LVAIYAADVL KSHPGATIIA DVKASQTLFD EIARLGGNPL
     MWKTGHSLLK AKMAETGSPL AGEMSGHIFF ADKWYGFDDA LYCAVRLIGL VSKLNQPLSE
     LRDRLPDVVN TPETRFQVSE ERKFQVVQEV EGRSSRLMAE GADVNDIDGV RVKDADGWWL
     LRASNTQDVL VARAESGTRR SWERLKGMVV AHWKPPASRP FLRGRRQLH
//