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Database: UniProt
Entry: F5T2V3_9GAMM
LinkDB: F5T2V3_9GAMM
Original site: F5T2V3_9GAMM 
ID   F5T2V3_9GAMM            Unreviewed;       495 AA.
AC   F5T2V3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:EGL53314.1};
GN   ORFNames=MAMP_00801 {ECO:0000313|EMBL:EGL53314.1};
OS   Methylophaga aminisulfidivorans MP.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL53314.1, ECO:0000313|Proteomes:UP000003544};
RN   [1] {ECO:0000313|EMBL:EGL53314.1, ECO:0000313|Proteomes:UP000003544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX   PubMed=21685284; DOI=10.1128/JB.05403-11;
RA   Han G.H., Kim W., Chun J., Kim S.W.;
RT   "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL   J. Bacteriol. 193:4265-4265(2011).
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:EGL53314.1}.
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DR   EMBL; AFIG01000003; EGL53314.1; -; Genomic_DNA.
DR   RefSeq; WP_007146564.1; NZ_AFIG01000003.1.
DR   AlphaFoldDB; F5T2V3; -.
DR   STRING; 1026882.MAMP_00801; -.
DR   eggNOG; COG1109; Bacteria.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000003544; 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; 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   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; 3.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003544}.
FT   DOMAIN          14..142
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          174..270
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          275..389
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          425..488
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   495 AA;  54459 MW;  2C1456119EF900C6 CRC64;
     MKIHIEQLMS DSGVKFGTSG TRGLVTDMTD RVCFAYTAAF LQHLIAGNQI QTGDEFGIGG
     DLRLSSPRIM NAVAKACQYY GLRPVNLGFI PSPAVALYGI QHKMPTIMVT GSHIPDDRNG
     MKFNLPIGEI LQADEQAIKQ QFVDIPDELF NNDGHFIKQD DVFAEPSLLA ETLYIERFSH
     FFPENCLSGM TIGIYQHSAV GRDLLQQILS VLGANTICLG RSEQFVSVDT EAIRPEDVQL
     AQQWASKHEL DAIVSTDGDS DRPLISDEKG RWLRGDIVGL LTAIYLAADI VVTPVSSNSA
     VNADFFEQVI RTRIGSPYVI SAMQTTVGES KKRIVGYEAN GGFLQQSAIE LAGNTLSPLP
     TRDAVIVILS VLLLAKQRQQ SVSELNSSMP AIYTSSDRLK NFALEKSRLL LETLLPDNEL
     SREQVKQLFP FMGEVKAVDT TDGVRMSFAD DEIIHIRPSG NAPELRCYIE ANHEKRAIAL
     NQQALDAIQL WAGSV
//
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