ID A0A1X1MPP5_9VIBR Unreviewed; 478 AA.
AC A0A1X1MPP5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ORT49381.1};
GN ORFNames=ST37_13295 {ECO:0000313|EMBL:ORT49381.1};
OS Vibrio sp. qd031.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1603038 {ECO:0000313|EMBL:ORT49381.1, ECO:0000313|Proteomes:UP000193432};
RN [1] {ECO:0000313|EMBL:ORT49381.1, ECO:0000313|Proteomes:UP000193432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORT49381.1, ECO:0000313|Proteomes:UP000193432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA Chen G.;
RT "Denovo assembling a bacteria genome.";
RL Submitted (MAY-2017) 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:ORT49381.1}.
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DR EMBL; JXQD01000025; ORT49381.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1MPP5; -.
DR STRING; 1603038.ST37_13295; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000193432; 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; cd03088; ManB; 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 PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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 SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
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:UP000193432}.
FT DOMAIN 14..131
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 163..260
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 281..381
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 417..473
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 478 AA; 51579 MW; 067DE8D303B1CD70 CRC64;
MTTVSTVIEQ GNIAFGTSGA RGLVSDFTAP ICAAFTLGFL TSQQSKSVVI GIDNRPSSPL
IASYCAFAAQ SLGYQVEYCG VLPTPALAAY AMSLNIPSIM ITGSHIPFDR NGIKFYRADG
EISKADEQAI IGNQYQLDAP LIAELSGIDQ HSLPKASHSA SQYYIERYTK LFANNTLKNK
RIGIYEHSSA GRDLYATLFE RLGATTLSLG RSDEFVPIDT EAVAAEDIEQ AKRWVTEHQL
DAVFSTDGDG DRPLLSDESG EYLRGDILGL LAAKALGIDS LALPVSCNTS VEGCGEFTQI
MRTKIGSPYV IEAFDTLCQT SRCVAGFEAN GGFLLASELT INGQALPALP TRDAVLPVIA
LLSYVEHSSI QDQVAALPKR YTAADRLQGI EREMSAQLLE QALIDDAAFL QSVGLAHLQV
VDVDQTDGLR LQLSDQSYLH LRPSGNAPEL RCYVETESPH SSQQRVDAVL AAISNQRR
//
