ID E4NWF0_HALBP Unreviewed; 441 AA.
AC E4NWF0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:ELY26258.1};
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ADQ69370.1};
GN OrderedLocusNames=Hbor_36640 {ECO:0000313|EMBL:ADQ69370.1};
GN ORFNames=C499_12395 {ECO:0000313|EMBL:ELY26258.1};
OS Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM 10706 /
OS KCTC 4070 / PR3).
OG Plasmid pHBOR04 {ECO:0000313|EMBL:ADQ69370.1,
OG ECO:0000313|Proteomes:UP000006663}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halogeometricum.
OX NCBI_TaxID=469382 {ECO:0000313|EMBL:ADQ69370.1, ECO:0000313|Proteomes:UP000006663};
RN [1] {ECO:0000313|Proteomes:UP000006663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / KCTC 4070 / PR3
RC {ECO:0000313|Proteomes:UP000006663};
RC PLASMID=pHBOR04 {ECO:0000313|Proteomes:UP000006663};
RX PubMed=21304651; DOI=10.4056/sigs.23264;
RA Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A.,
RA Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Anderson I.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.;
RT "Complete genome sequence of Halogeometricum borinquense type strain
RT (PR3).";
RL Stand. Genomic Sci. 1:150-159(2009).
RN [2] {ECO:0000313|EMBL:ADQ69370.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PR 3 {ECO:0000313|EMBL:ADQ69370.1};
RC PLASMID=pHBOR04 {ECO:0000313|EMBL:ADQ69370.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Mikhailova N., Anderson I., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Tindal B., Klenk H.-P., Eisen J.A.;
RT "The complete plasmid4 of Halogeometricum borinquense DSM 11551.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ELY26258.1, ECO:0000313|Proteomes:UP000011585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11551 {ECO:0000313|EMBL:ELY26258.1,
RC ECO:0000313|Proteomes:UP000011585};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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; CP001694; ADQ69370.1; -; Genomic_DNA.
DR EMBL; AOHT01000040; ELY26258.1; -; Genomic_DNA.
DR RefSeq; WP_006055786.1; NZ_AOHT01000040.1.
DR AlphaFoldDB; E4NWF0; -.
DR GeneID; 9989296; -.
DR KEGG; hbo:Hbor_36640; -.
DR PATRIC; fig|469382.19.peg.2446; -.
DR HOGENOM; CLU_016950_7_1_2; -.
DR OrthoDB; 10363at2157; -.
DR Proteomes; UP000006663; Plasmid pHBOR04.
DR Proteomes; UP000011585; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03087; PGM_like1; 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 InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR024086; GlmM_arc-type.
DR NCBIfam; TIGR03990; Arch_GlmM; 1.
DR PANTHER; PTHR42946:SF6; PHOSPHOGLUCOSAMINE MUTASE; 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 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 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 Plasmid {ECO:0000313|EMBL:ADQ69370.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006663}.
FT DOMAIN 2..127
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 148..241
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 247..349
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 363..434
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 441 AA; 46362 MW; 55BC9E725E376B67 CRC64;
MFGTSGIRGP VGETVTADLA LHIGQAVAVE ADRAVVGRDA RVTGDVLADA LSVGLRECGT
DVIRVGVAAT PTIARSVEWF GADVGVAITA SHNPAADNGI KLWNESGQAF SPTQNERIER
RLDNDDSARA TWDSFGSEST DRSAVERHVS AITDEFDSMT GLNAVVDLGN GTGRVTVDAL
YELGATVNTL DAQPDGTFPA RKSEPNAETL TTLQRTVPAL DADFGIAHDG DSDRMVAVSD
TGEYVPGDVL LALFARDAVS PGDSVAVPVD TSLLVADVVA SAGGTVVYTP VGDVYIAEAV
SQSGFVFGGE PSGAWIWPDQ TLAPDANYAA LRLADLIRRE GPLSEQVADI AASRYTTRRL
SLPVDDKASA MRAIDGLLSA KYDDIDTTDG VRVDTDDGWL LVRASGTEPL VRVTAEARQE
SKADALLEEV TSLIEKEEIT T
//
