GenomeNet

Database: UniProt
Entry: A0A1E7ZE17_9ALTE
LinkDB: A0A1E7ZE17_9ALTE
Original site: A0A1E7ZE17_9ALTE 
ID   A0A1E7ZE17_9ALTE        Unreviewed;       486 AA.
AC   A0A1E7ZE17;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE            EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN   ORFNames=BFC18_06225 {ECO:0000313|EMBL:OFC71747.1};
OS   Alteromonas confluentis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1656094 {ECO:0000313|EMBL:OFC71747.1, ECO:0000313|Proteomes:UP000175691};
RN   [1] {ECO:0000313|EMBL:OFC71747.1, ECO:0000313|Proteomes:UP000175691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42603 {ECO:0000313|EMBL:OFC71747.1,
RC   ECO:0000313|Proteomes:UP000175691};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) 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:OFC71747.1}.
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; MDHN01000010; OFC71747.1; -; Genomic_DNA.
DR   RefSeq; WP_070124086.1; NZ_MDHN01000010.1.
DR   AlphaFoldDB; A0A1E7ZE17; -.
DR   STRING; 1656094.BFC18_06225; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000175691; 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:UP000175691}.
FT   DOMAIN          8..134
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          183..287
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          292..401
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          407..479
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   486 AA;  52848 MW;  C281FD75054A6A6F CRC64;
     MSQPITCFKA YDIRGELNTQ LSEEVAYRIG RGFATELNAK TVVVGGDVRL TSTPLKLALA
     AGLIDGGATV LDLGDTGTEE IYFATKHLGV DGGIEVTASH NPINYNGMKM VKAGSVPISG
     DTGLNAIKDA AEALDDSLVA ERLAFYCNGE TIDADAFFNG KAHVSTDKLN ASGQYELKDC
     LTDYAEHVVS YIDTANLTPL KIVANSGNGA AGKALDAIEA VFKAKGVPVE FIKVHHQPDG
     TFPNGIPNPL LPENRDDTAQ AVIDSKADFG IAWDGDFDRC FLFDANGVFI EGYYIVGLLA
     QAFIDKEADA KIIYDPRVFW NTEDIVKSAG GIPIKSKTGH AFIKERMRKE DAVYGGEMSA
     HHYFRDFAYC DSGMIPWLLV AELLCTKQIS LADMVKARIE AFPSSGEINS KLKDADAALA
     RIKQKYEADA LVIDDTDGIG YEFAEWRFNL RKSNTEPVIR LNVESKGDIP LMEAKTEELI
     TLIRSE
//
DBGET integrated database retrieval system