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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//