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Database: UniProt
Entry: A0A1S9ZXU2_9GAMM
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ID   A0A1S9ZXU2_9GAMM        Unreviewed;       472 AA.
AC   A0A1S9ZXU2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE            EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN   Name=algC {ECO:0000313|EMBL:STZ10547.1};
GN   ORFNames=B0181_09550 {ECO:0000313|EMBL:OOR87791.1}, NCTC10293_00888
GN   {ECO:0000313|EMBL:STZ10547.1};
OS   Moraxella caviae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=34060 {ECO:0000313|EMBL:OOR87791.1, ECO:0000313|Proteomes:UP000190435};
RN   [1] {ECO:0000313|EMBL:OOR87791.1, ECO:0000313|Proteomes:UP000190435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 355 {ECO:0000313|EMBL:OOR87791.1,
RC   ECO:0000313|Proteomes:UP000190435};
RA   Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA   Karlsson R., Boulund F., Engstrand L., Moore E.;
RT   "Draft genome sequence of Moraxella caviae CCUG 355 type strain.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:STZ10547.1, ECO:0000313|Proteomes:UP000255279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10293 {ECO:0000313|EMBL:STZ10547.1,
RC   ECO:0000313|Proteomes:UP000255279};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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; Evidence={ECO:0000256|ARBA:ARBA00000586};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC       step 2/2. {ECO:0000256|ARBA:ARBA00004699}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; MUXU01000062; OOR87791.1; -; Genomic_DNA.
DR   EMBL; UGQE01000001; STZ10547.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9ZXU2; -.
DR   STRING; 34060.B0181_09550; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000190435; Unassembled WGS sequence.
DR   Proteomes; UP000255279; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase 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; 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.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:STZ10547.1};
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:UP000190435}.
FT   DOMAIN          12..145
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          162..264
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          269..374
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          415..462
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   472 AA;  51121 MW;  8436F22E5785B463 CRC64;
     MKNFEPITIS CFKAYDVRGE LDVNLDADIA YRIGRAFGQI LASQNNTPNP TIVVGSDIRP
     TSHTLKTAAA EGITDAGVNV IDLGMTGTEE VYFATSHFGA IGGLEVTASH NPINYNGMKL
     VRENSRPISA DTGLGEIRAL AESGQFASAA KGQITQNTDK AAYIDKLMSF VDTAKFTAKK
     IVVNSGNGSA GPVVDELEKR LANLPIELIK VHHEPDGTFP NGIPNPMIIA NQKSTQQAVI
     AHKADFGVAF DGDFDRCFLF DEKGDFIEGS YIVGMLAEAF LGKHEGASIV YDPRVIYNTE
     NVIKTFGGTP QISKSGHSFI KQVMRETGGI YGGEMSAHHY FKDFFYCDSG MIPWLLVIEL
     LSTTGKTLSE LVDGYIAAFP SSGELNFRLG AMSADEICRT LEAKFGTLNP AKNTLDGLSL
     DFGQWRFNLR SSNTEPLIRL NIESKGDKAL LQEKTDEILA ILHDCGAVAA DH
//
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