ID A0A084IM05_SALHC Unreviewed; 452 AA.
AC A0A084IM05;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=C41B8_07975 {ECO:0000313|EMBL:KEZ77739.1};
OS Salinisphaera hydrothermalis (strain C41B8).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC Salinisphaeraceae; Salinisphaera.
OX NCBI_TaxID=1304275 {ECO:0000313|EMBL:KEZ77739.1, ECO:0000313|Proteomes:UP000028302};
RN [1] {ECO:0000313|EMBL:KEZ77739.1, ECO:0000313|Proteomes:UP000028302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C41B8 {ECO:0000313|EMBL:KEZ77739.1,
RC ECO:0000313|Proteomes:UP000028302};
RA Li C., Lai Q., Shao Z.;
RT "Salinisphaera hydrothermalis C41B8 Genome Sequencing.";
RL Submitted (MAR-2013) 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}.
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:KEZ77739.1}.
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DR EMBL; APNK01000009; KEZ77739.1; -; Genomic_DNA.
DR RefSeq; WP_037336434.1; NZ_APNK01000009.1.
DR AlphaFoldDB; A0A084IM05; -.
DR STRING; 1304275.C41B8_07975; -.
DR PATRIC; fig|1304275.5.peg.1626; -.
DR eggNOG; COG1109; Bacteria.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000028302; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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};
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:UP000028302}.
FT DOMAIN 8..135
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 152..252
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 257..365
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 372..444
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 452 AA; 49739 MW; D296F52EB4700C08 CRC64;
MGQYYPFFKA YDVRARVPEE LDADMARRIG LAFAAELGAK TVVVGRDMRL SSPELADALI
DGLTTAGADV LDIGLCGTEE VYYGVFSQNA DGGVMVTASH NPKDYNGLKF VREQAKPISA
DTGLADIERR VHANDVSPAA TPGERRPLDQ RDAYVAFLLA QIKPENFKPL KIVVNPGNGC
AGLVVEKLAE KLPFEFVRMQ FEPDGELPNG VPNPLLVENR EATSKVVRDA GADFGVAWDG
DFDRCFFFDE HGEFIEGYYI VGLIAQMLLK MNPGEAIVHD PRLIWNTLAQ VEEAGGRAVE
SKSGHSFMKQ VMRENDALYG GEMSAHHYFR EFSYADNGHL PWLVIAQLIS ETGKGLSTLV
KERIAAFPAS GEINRKVDDA DAVMADMEAH YADSAQSVEH VDGLSMDFGD WRFNLRKSNT
EPVIRLNVET RGDKALMQEK TDELLARIGG TA
//