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Database: UniProt
Entry: A0A2V4WVV9_9FLAO
LinkDB: A0A2V4WVV9_9FLAO
Original site: A0A2V4WVV9_9FLAO 
ID   A0A2V4WVV9_9FLAO        Unreviewed;       575 AA.
AC   A0A2V4WVV9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:PYE81090.1};
GN   ORFNames=DFQ11_103170 {ECO:0000313|EMBL:PYE81090.1};
OS   Winogradskyella epiphytica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=262005 {ECO:0000313|EMBL:PYE81090.1, ECO:0000313|Proteomes:UP000248054};
RN   [1] {ECO:0000313|EMBL:PYE81090.1, ECO:0000313|Proteomes:UP000248054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7945 {ECO:0000313|EMBL:PYE81090.1,
RC   ECO:0000313|Proteomes:UP000248054};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUN-2018) 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, 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:PYE81090.1}.
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DR   EMBL; QJTD01000003; PYE81090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V4WVV9; -.
DR   Proteomes; UP000248054; 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; cd05799; PGM2; 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; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR017880; KilA_N.
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   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR   PROSITE; PS51301; KILA_N; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|RuleBase:RU004326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248054}.
FT   DOMAIN          1..31
FT                   /note="KilA-N"
FT                   /evidence="ECO:0000259|PROSITE:PS51301"
SQ   SEQUENCE   575 AA;  64534 MW;  9B879F0AF1507F07 CRC64;
     MIYIKPEILE RVNTWLTPTF DEESQKQIKE MIASNPKELE ESFYKDLEFG TGGMRGIMGL
     GTNRINKYTL GKNTQGLSNY LQQTFPNEDL KVAIAYDCRH NSKTFGKLVA DVFSANGIKV
     YLFEDLRPTP ELSFTLKHLN CHCGIVLTAS HNPPEYNGYK VYWQDGGQLV PPQDAEIIAE
     INRLKYSEIK FEANESLIQY IGKDIDDVFI NASVNNGSFD TTKEAKENLN IVFTSLHGTS
     IIAIPETLKR AGYTNVNIVE EQREPDGDFP TVVSPNPEEP EALKMAMALA EKVNGDIVIG
     TDPDCDRLGV VVRNLDNELV ILNGNQTMLL MTNFLLKQWK NEGKIKGNEF IASTIVSTPM
     MSVIADAYDV ECKIGLTGFK WIAKMIKDFP NLDFIGGGEE SFGFMVGDFV RDKDAVTSTL
     LACEIAAQAK AKGKTMFEEL IDIYIKHGFY KERLVSLTKK GIEGAEEIKQ MMIDARNNPL
     KEINGEKVVL IEDYQTSIAK NLQSQEESTL DIPKSNVLIY YTENGSKIAL RPSGTEPKIK
     FYISVNTELD NSSDFKKTEQ LLDDRIDAIL KDMNL
//
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