ID A0A241W9D7_9GAMM Unreviewed; 456 AA.
AC A0A241W9D7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=B9T35_14860 {ECO:0000313|EMBL:OTG90608.1};
OS Acinetobacter sp. ANC 3832.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1977874 {ECO:0000313|EMBL:OTG90608.1, ECO:0000313|Proteomes:UP000194704};
RN [1] {ECO:0000313|EMBL:OTG90608.1, ECO:0000313|Proteomes:UP000194704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 3832 {ECO:0000313|EMBL:OTG90608.1,
RC ECO:0000313|Proteomes:UP000194704};
RA Nemec A., Radolfova-Krizova L.;
RT "High diversity of culturable Acinetobacter species in natural soil and
RT water ecosystems.";
RL Submitted (APR-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, 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:OTG90608.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NEGJ01000013; OTG90608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A241W9D7; -.
DR STRING; 1977874.B9T35_14860; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000194704; 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}.
FT DOMAIN 7..134
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 152..256
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 261..371
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 376..438
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 456 AA; 51039 MW; 980438A3E105AA8F CRC64;
MTTLTCFKAY DIRGKLGSEL NEEIAYKIGR AYGQIHQPKT VVVGCDIRLS SEGLKQATIK
GLNDAGVNVL DLGMTGTEEV YFGAFHLDVQ GGIEITASHN PMDYNGLKLV RENARPISAN
TGLKEIQALA ESNAFIDVEK KGNTEKYNIL PEFIDHLMTY IDPRKIRPLK LVMNAGNGAA
GHVVDAIEEK FKQLNIPIEF IKIHNEADGT FPNGIPNPIL IENRDSTRNA VLIHHADMGI
AWDGDFDRCF LFDEKGQFIE GYYIVGLLAQ AFLLKQSGEK IVHDPRLVWN TLAIVDEYNG
VAVQSKSGHA FIKDVMREHN AVYGGEMSAH HYFRDFSYCD SGMIPWLLAV VVLSETKQSL
SSLVEDMITK FPCSGEINFK VQDTQETIQK IFDHFAEQKP TIDQTDGVSL DFGTWRLNVR
ASNTEPLLRL NIESRLDRNP EPMQAYVDEL TQLIQG
//
