ID A0A0S8HH93_9BACE Unreviewed; 469 AA.
AC A0A0S8HH93;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Phosphoglucosamine mutase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMS27_12885 {ECO:0000313|EMBL:KPK83421.1};
OS Bacteroides sp. SM23_62_1.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1703353 {ECO:0000313|EMBL:KPK83421.1, ECO:0000313|Proteomes:UP000051265};
RN [1] {ECO:0000313|EMBL:KPK83421.1, ECO:0000313|Proteomes:UP000051265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_62_1 {ECO:0000313|EMBL:KPK83421.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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:KPK83421.1}.
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DR EMBL; LJUQ01000144; KPK83421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8HH93; -.
DR PATRIC; fig|1703353.3.peg.538; -.
DR Proteomes; UP000051265; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR036900; A-D-PHexomutase_C_sf.
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; 2.
PE 3: Inferred from homology;
FT DOMAIN 4..137
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 164..260
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 264..373
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 469 AA; 53412 MW; 5D88E768871E633A CRC64;
MDRIKFGTDG WRGIIAGNFT VANVARLTDA VALWLLNKYR ETSVVIGYDT RFGGKLFAGT
AARVLAMKGI KVYLSSDFVT SPMVSYAVTW YGAGLGIMIT ASHYAFEYSG YKIKGEHGGP
MMEEDIRNIE ALVSNDMNID LERIKWQNLV EQKTIEYVNI ASIYFERIKS NFDLDLIKKS
GLRLAFDAMY GSSQNIIKQL LPGVKNFHCK TDPFFNHIPP EPTEENLKEF IDMIRSDGNF
SCGLAIDGDG DRLALIDNRG NYIDSNHILL ILIHCLAAYR RLRGKVIIGY SSTSRAEKIC
KHYGIDLQRV KIGFKEICRV MLKEDILVGG EESGGIGMRN HVPDRDGIWI GLTIWQFMAE
TRKSLDQLIN EVYAITGRFS SERKNIETGK EQQLRIIEDC TKGIYQSFKD YRILRTEQFD
GFKFWLEKDQ WAMIKPSGTE SKFWIYAESE TREQALSILQ AVCETIQNT
//
