ID A0A410G6Y0_9FLAO Unreviewed; 582 AA.
AC A0A410G6Y0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Phospho-sugar mutase {ECO:0000313|EMBL:QAA83044.1};
GN ORFNames=EI546_15560 {ECO:0000313|EMBL:QAA83044.1};
OS Aequorivita sp. H23M31.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=2494375 {ECO:0000313|EMBL:QAA83044.1, ECO:0000313|Proteomes:UP000285517};
RN [1] {ECO:0000313|EMBL:QAA83044.1, ECO:0000313|Proteomes:UP000285517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H23M31 {ECO:0000313|EMBL:QAA83044.1,
RC ECO:0000313|Proteomes:UP000285517};
RA Bae J.-W.;
RT "Complete genome sequencing of Aequorivita sp. H23M31.";
RL Submitted (JAN-2019) 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}.
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DR EMBL; CP034951; QAA83044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410G6Y0; -.
DR KEGG; aev:EI546_15560; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000285517; Chromosome.
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; IPR005841; Alpha-D-phosphohexomutase_SF.
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 PRINTS; PR00509; PGMPMM.
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:UP000285517}.
FT DOMAIN 1..31
FT /note="KilA-N"
FT /evidence="ECO:0000259|PROSITE:PS51301"
SQ SEQUENCE 582 AA; 64936 MW; 3C7A8F97907CF9E4 CRC64;
MIYVDPKILA RVNQWLTPFF DEKIQHEIKE MIAHDPKKLE DTFYKNLEFG TGGMRGIMGA
GDNRINKYTL GKNTQGLSNY LKRQFPNQEI KVAIAFDCRH NSKEFAKLVA DVFSANGIKV
FLFSELRPTP ELSFAVKYLD CKAGIVLTAS HNPPEYNGYK VYWEDGGQLV PPQDGEIIAE
INSLKYQDTK FEANEDLIQL IDSEVDEAFA KASIENGTFG TSSEAKDNLK IVFTSLHGTS
ITMVPQVLDQ AAYKNVSIVK EQAEPDGDFP TVKSPNPEEP AALKMALDLA EKEHADIVIG
TDPDCDRLGV AVRNNENKME LLNGNQTMVL MTHFLLEQWK KAGKLNGKQF VASTIVSTPL
VEKIADHYGV KYIEGLTGFK WIAKMIKDYP ELEFIGGGEE SFGYLVGDFV RDKDAVTATL
LACEIAAQKK AEGSSMFQYM QDIYNEFGEY REHLISITKK GKEGAEEISA MMKELRENPF
KEIGGSKVSR MDDILIDKRT DFTSGKTTNL NLPKSNVLIY YTEDGSKIAA RPSGTEPKIK
FYISVTTGAS AKNSSVPQAE KENSDEILQK KIDAIKAQLN VH
//
