ID A0A2K9LMR7_9GAMM Unreviewed; 879 AA.
AC A0A2K9LMR7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=Kalk_10245 {ECO:0000313|EMBL:AUM12775.1};
OS Ketobacter alkanivorans.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Pseudomonadales; Ketobacteraceae; Ketobacter.
OX NCBI_TaxID=1917421 {ECO:0000313|EMBL:AUM12775.1, ECO:0000313|Proteomes:UP000235116};
RN [1] {ECO:0000313|Proteomes:UP000235116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GI5 {ECO:0000313|Proteomes:UP000235116};
RA Kim S.-J., Rhee S.-K.;
RT "Direct submision.";
RL Submitted (AUG-2017) 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}.
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DR EMBL; CP022684; AUM12775.1; -; Genomic_DNA.
DR RefSeq; WP_101894158.1; NZ_CP022684.1.
DR AlphaFoldDB; A0A2K9LMR7; -.
DR KEGG; kak:Kalk_10245; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000235116; Chromosome.
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; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR43771:SF2; PHOSPHOMANNOMUTASE_PHOSPHOGLUCOMUTASE; 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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000235116};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 429..555
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 575..671
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 676..785
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 794..866
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 879 AA; 95491 MW; AFF781363676F773 CRC64;
MVKKAKKSPA AAEPTSDAET TNPDTSKKAK SSIKSGLLAI MLPAIAGSAL AVAICGALLL
FLVIQPSANQ QMSLFGEAQA KQYLNELVQL GRSYQASVQQ VANSALVKDA ILADNSAIER
RQQQLMELFP AASNIHLFKK GKAAKDPDSV PPISFPQLDM VAKAEKKNNA APEIHQHDKK
SYLTIVKAIR EQDKTLGTLL VSFELSALRK NMSGLDPSLG YVEVIQTFSN QPVVMYSSGN
AQHKTGNGYE AKGDIPHWSA RFYPAADTNV IANNSAMVWV LVGLSVILVL GFSSASYFML
NRALQTNAMA MAAFFQSQLM REKTSKPFTL GIFASLAQTL SRLFDEYEVK QAKVLAKAKA
GTKSADDKPM PDFDPTYRNN DVLDLDLDND DDDLLSAAAD IDDNPLELDQ MEIAEPELAS
IDIKVSPLIF RAYDIRGIVG DTIDRDVAYA LGAAIGSEAK ECGQDAVIVA RDGRHSSSEL
AESLAEGLQS TGCDVIDIGM VPTPILYYAT KTQRTQSGVM VTGSHNPADY NGFKIVINDE
TLSKERIQGL RKRLDDGKLV KGQGRYEAID IAPEYLERIC SDVVLAKPMR IVVDTGNGVA
GPLTCQLLES LGCMVTPLYT DVDGDFPNHH PDPSVPENLE DLIRTVQAEG AELGLALDGD
GDRLGLVTAS GKIIWPDRML MLYARDLLAR NPGADVLYDV KCTRDVAELV SNLGGRAIMC
ATGHSLMKAK MKETGAVVGG ELSGHIFFND RWYGFDDALY SAARLLEILS MEPFEAEQVF
EEFPEKVSTP ELHIKVSEST KFKIMEKLES QGNFAGGNLV KVDGVRVDFP DSWGLIRASN
TTPVLVARFE GDTEAALENV KSVFREQLLA VEPSLNISF
//
