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Database: UniProt
Entry: A6F740_9GAMM
LinkDB: A6F740_9GAMM
Original site: A6F740_9GAMM 
ID   A6F740_9GAMM            Unreviewed;       474 AA.
AC   A6F740;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:EDM69067.1};
GN   ORFNames=PE36_06262 {ECO:0000313|EMBL:EDM69067.1};
OS   Moritella sp. PE36.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=58051 {ECO:0000313|EMBL:EDM69067.1, ECO:0000313|Proteomes:UP000004278};
RN   [1] {ECO:0000313|EMBL:EDM69067.1, ECO:0000313|Proteomes:UP000004278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PE36 {ECO:0000313|EMBL:EDM69067.1,
RC   ECO:0000313|Proteomes:UP000004278};
RA   Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., 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:EDM69067.1}.
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DR   EMBL; ABCQ01000001; EDM69067.1; -; Genomic_DNA.
DR   RefSeq; WP_006029907.1; NZ_ABCQ01000001.1.
DR   AlphaFoldDB; A6F740; -.
DR   STRING; 58051.PE36_06262; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000004278; 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}.
FT   DOMAIN          14..139
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          159..256
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          261..375
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          421..469
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   474 AA;  51505 MW;  99DC4D45AEEC80DE CRC64;
     MLISSNEIIK SGIQFGTSGA RGLVTQFTDN ACAAFTHAFI SCIKKQFTFK QVAIAIDNRP
     SSPAMAQACI KALEQLGIEA IYYGVVPTPA LAYISMQDNI PCIMVTGSHI PFDRNGLKFY
     RPDGEISKAD EQGILNATAE FEAISDLPEL VTNTKAAVAY VERYTSLFDS TLLAGKRVGI
     YEHSSAGRDL YADMFIALGA DVIALERSDV FVPIDTEAVS EADKLKAKNW SAQYDLDFIF
     STDGDGDRPL VADENGDWLR GDVLGLLCAN AMKIEALAVP VSCNTAIESC ELFSHVTRTK
     IGSPYVIAEF EQLAKDYDSV AGFEANGGFL LGSDVVVNNK IVKALPTRDA VLPALMLLAA
     ASENNISALV NTLPQRMTHS DRIQNFATEK SLAILKVAKE QPEYFLTQLG FSEFVVAGID
     TTDGLRMTLM NGDIIHFRPS GNAPELRCYA ESNSIEQAQD LVNQALQQIQ FIKS
//
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