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Database: UniProt
Entry: A0A238LHX7_9RHOB
LinkDB: A0A238LHX7_9RHOB
Original site: A0A238LHX7_9RHOB 
ID   A0A238LHX7_9RHOB        Unreviewed;       461 AA.
AC   A0A238LHX7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:SMY09228.1};
DE            EC=5.4.2.10 {ECO:0000313|EMBL:SMY09228.1};
GN   Name=glmM_2 {ECO:0000313|EMBL:SMY09228.1};
GN   ORFNames=LOM8899_03393 {ECO:0000313|EMBL:SMY09228.1};
OS   Flavimaricola marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Flavimaricola.
OX   NCBI_TaxID=1819565 {ECO:0000313|EMBL:SMY09228.1, ECO:0000313|Proteomes:UP000201613};
RN   [1] {ECO:0000313|EMBL:SMY09228.1, ECO:0000313|Proteomes:UP000201613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8899 {ECO:0000313|EMBL:SMY09228.1,
RC   ECO:0000313|Proteomes:UP000201613};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) 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, ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; FXZK01000008; SMY09228.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238LHX7; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000201613; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-EC.
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   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOSAMINE MUTASE FAMILY PROTEIN; 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.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:SMY09228.1};
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:UP000201613}.
FT   DOMAIN          4..125
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          147..244
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          261..338
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          398..453
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   461 AA;  46805 MW;  8EABA03A29FAB6FA CRC64;
     MPPKFGTSGL RGLVTELTET LVADHVAAFI SACPTGTGLF IGQDLRSSSP MLADVVARTG
     QAAGLAVTDC GAVPTPALAM ASMQAGAAAV MITGSHIPDD RNGLKFYTPE GEITKEHEAA
     ILATLGTSSG AATAGPAPAS NTGANAAYIA RYVTAFGPEA LAGLTIGVYS HSAVGRDVLI
     EAFQALGAKT LELGRADRFI PVDTEAVDAE TRAQLAAWAA EHPLDAIAST DGDGDRPLMT
     DETGRVIVGD VLGQITGAML GAEVAVTPVS SNTGAEAGGA FGRVIRTRIG SPFVIAGMEQ
     AGGKVVGYEA NGGFLLGFEA QGPAGPLPPL MTRDALLPLI APLVQARGAG GLAALVAAQP
     PRFTAADRLQ EVPTERSLAL VASLSSSAEE RARFLASFEG SEARIDQTDG LRITMTDGRI
     VHLRPSGNAP ELRFYGEADS AAAAEALLAE GLAILRAAVD G
//
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