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Database: UniProt
Entry: A6D7U6_9VIBR
LinkDB: A6D7U6_9VIBR
Original site: A6D7U6_9VIBR 
ID   A6D7U6_9VIBR            Unreviewed;       470 AA.
AC   A6D7U6;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:EDL51316.1};
GN   ORFNames=VSAK1_08039 {ECO:0000313|EMBL:EDL51316.1};
OS   Vibrio mediterranei AK1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=391591 {ECO:0000313|EMBL:EDL51316.1, ECO:0000313|Proteomes:UP000003769};
RN   [1] {ECO:0000313|EMBL:EDL51316.1, ECO:0000313|Proteomes:UP000003769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK1 {ECO:0000313|EMBL:EDL51316.1,
RC   ECO:0000313|Proteomes:UP000003769};
RA   Rosenberg E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
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:EDL51316.1}.
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DR   EMBL; ABCH01000063; EDL51316.1; -; Genomic_DNA.
DR   RefSeq; WP_006075052.1; NZ_ABCH01000063.1.
DR   AlphaFoldDB; A6D7U6; -.
DR   Proteomes; UP000003769; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05800; PGM_like2; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR   PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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; 2.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          2..136
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          162..262
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          267..378
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          421..467
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   470 AA;  52301 MW;  86B0D023DB18B38E CRC64;
     MIKFGTGGWR AFIGEEFTRD NVKLVAQALA NIINDENVAE RGFIIGYDRR FLSDKAGRWF
     AEVLAANQIP VHFINKFVPT PIVMFKAKSM NCAYSACITA SHNPADYNGI KVFIEGGRDA
     DEVITEKIES QIATLTATEV KSIDFEHAVD NQQIIEINPM NEFVDSIIEL IDIESIKKAN
     LRVLIDPMFG VAKNALQTVL INGRCDVDVI NDGKNPDFGG LMPSPSAATL YRLKHLVAAE
     GYDIGIGTDG DADRLGIIDE KGNFIHPNEV LMLLYYYLLE YKGWKGSVVR NIATTHLLDK
     IAQSYGEKSF EVPVGFKHIS AQMEADDSLI GGESSGGLTI RGHIKGKDGV FASSLLVEML
     SVTNKKLSEL LDEIYSKYGY AYTAEGDCTF KPAQKDSLYH KIYVEKSLPE FDYEVEKVSY
     SDGAKVYFKN GGWVIARFSG TEPLLRIFCE MEDKAQAEYV LQQMKDFLSL
//
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