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Database: UniProt
Entry: K2HNT2_9RHOB
LinkDB: K2HNT2_9RHOB
Original site: K2HNT2_9RHOB 
ID   K2HNT2_9RHOB            Unreviewed;       459 AA.
AC   K2HNT2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Phosphoglucomutase/phosphomannomutase {ECO:0000313|EMBL:EKE44519.1};
GN   ORFNames=OCGS_1357 {ECO:0000313|EMBL:EKE44519.1};
OS   Oceaniovalibus guishaninsula JLT2003.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Oceaniovalibus.
OX   NCBI_TaxID=1231392 {ECO:0000313|EMBL:EKE44519.1, ECO:0000313|Proteomes:UP000006765};
RN   [1] {ECO:0000313|EMBL:EKE44519.1, ECO:0000313|Proteomes:UP000006765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLT2003 {ECO:0000313|EMBL:EKE44519.1,
RC   ECO:0000313|Proteomes:UP000006765};
RX   PubMed=23144420; DOI=10.1128/JB.01874-12;
RA   Tang K., Liu K., Jiao N.;
RT   "Draft Genome Sequence of Oceaniovalibus guishaninsula JLT2003T.";
RL   J. Bacteriol. 194:6683-6683(2012).
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   -!- 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:EKE44519.1}.
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DR   EMBL; AMGO01000021; EKE44519.1; -; Genomic_DNA.
DR   RefSeq; WP_007426509.1; NZ_AMGO01000021.1.
DR   AlphaFoldDB; K2HNT2; -.
DR   STRING; 1231392.OCGS_1357; -.
DR   PATRIC; fig|1231392.3.peg.1361; -.
DR   eggNOG; COG1109; Bacteria.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000006765; Unassembled WGS sequence.
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; 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; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
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; PF00408; PGM_PMM_IV; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000006765}.
FT   DOMAIN          4..125
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          150..244
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          402..449
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   459 AA;  46868 MW;  245380F929561683 CRC64;
     MPPKFGTSGL RGLAVELTDS LIAAHVRAFA SVCDSGGTVC IGRDLRDSSP RIAAAVGQAA
     RKAGLDTVDC GLVPTPALAM AALDAGAGAI MVTGSHIPAD RNGLKFYTRA GEITKQEEAA
     ITAALSGTPP AADGTGRGSD DPQAGARFAA RYVDAFGAGA LTGRRIGIFS HSAVGRDLLA
     DMLRGLGAVT VELGRSDTFI PVDTEAVDPA ARAQLAAWTS EHDLHAIAST DGDSDRPMLC
     DEKGRMIAGD VLGQIVAETL GARTVVTPVS SNTGAERKGF DAVIRTRIGS PHVIAAMQDA
     MRDGALNVAG YEANGGFLLG FAADAPGGTL SPLMTRDSFL PIVAAGDAPL SQRVGAEPAR
     FTATDRVQDV PTNRSLALVA RLTDDGAARS QFAGRAGLAG GIRADVTDGL RLTDGDGNII
     HLRPSGNAPE LRVYAEADTP ARAETLLAQG MGAVRGLVS
//
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