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Database: UniProt
Entry: E1X5I1_HALMS
LinkDB: E1X5I1_HALMS
Original site: E1X5I1_HALMS 
ID   E1X5I1_HALMS            Unreviewed;       589 AA.
AC   E1X5I1;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:CBW27302.1};
GN   Name=pgmA {ECO:0000313|EMBL:CBW27302.1};
GN   OrderedLocusNames=BMS_2512 {ECO:0000313|EMBL:CBW27302.1};
OS   Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS   (Bacteriovorax marinus).
OC   Bacteria; Bdellovibrionota; Bacteriovoracia; Bacteriovoracales;
OC   Halobacteriovoraceae; Halobacteriovorax.
OX   NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW27302.1, ECO:0000313|Proteomes:UP000008963};
RN   [1] {ECO:0000313|Proteomes:UP000008963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-682 / DSM 15412 / SJ
RC   {ECO:0000313|Proteomes:UP000008963};
RX   PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA   Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA   Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA   Williams H.N., Stine O.C.;
RT   "A small predatory core genome in the divergent marine Bacteriovorax
RT   marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL   ISME J. 7:148-160(2013).
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; FQ312005; CBW27302.1; -; Genomic_DNA.
DR   RefSeq; WP_014245078.1; NC_016620.1.
DR   AlphaFoldDB; E1X5I1; -.
DR   STRING; 862908.BMS_2512; -.
DR   KEGG; bmx:BMS_2512; -.
DR   PATRIC; fig|862908.3.peg.2397; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_0_7; -.
DR   Proteomes; UP000008963; 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   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   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; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Magnesium {ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|RuleBase:RU004326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008963}.
FT   DOMAIN          47..187
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          216..324
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          331..452
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   COILED          557..584
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   589 AA;  66280 MW;  C32908E654674DD7 CRC64;
     MEQSALERAT AWANNKYFSE ESRKEIQNLI DENNEKELIE RFYKDLEFGT GGMRSIIGAG
     TNRINTYTIR KATQALANEV IRSGKEEGLS ELKVAISYDN RRFSFEFAKE VASVMAANGI
     HAYIYKRLNP VPLLSFSVRH HNAQAGVMVT ASHNPPEYNG YKVFWNDGAQ VTPPNDSNII
     NNYNSITDFA SVKTMDFQEG ESKGLIHWVG EDVENKYFES INSKAINPEM CSENGGKLNI
     VYTPIHGTGY IPCTTALSNL GFSNVQVVEE QKLPDSDFPT VSSPNPENPE ALAMAVKLMQ
     DTKADVAFGT DPDTDRVGLA FEKNGEMVYL NGNQIGILMV HYMMNGLTKS GKMPTNPYFV
     KTIVTTPLQD QIAKSFGVET FNTLTGFKWI CGKMNQLEKT NPEKNFVFAT EESFGYLNHE
     FVRDKDGVSS ITLLSEICLH YKLQGMDLVD GLDKIYEEYG FSSETLLNLN YFGKEGSEKI
     SRIMDNFRGY SEKTFCGEEI SYLEDYSTGE SKSFTDSKIS KLDLPSSNVL GFNFTNGTKV
     YMRPSGTEPK IKFYIMIQEK EGSLEEKKQK ANQKTQEFLD YIKEQADQA
//
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