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Database: UniProt
Entry: A0A0K2M5A3_9NOST
LinkDB: A0A0K2M5A3_9NOST
Original site: A0A0K2M5A3_9NOST 
ID   A0A0K2M5A3_9NOST        Unreviewed;       480 AA.
AC   A0A0K2M5A3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:ALB43253.1};
GN   ORFNames=AA650_24895 {ECO:0000313|EMBL:ALB43253.1};
OS   Anabaena sp. WA102.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=1647413 {ECO:0000313|EMBL:ALB43253.1, ECO:0000313|Proteomes:UP000056652};
RN   [1] {ECO:0000313|EMBL:ALB43253.1, ECO:0000313|Proteomes:UP000056652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA102 {ECO:0000313|EMBL:ALB43253.1,
RC   ECO:0000313|Proteomes:UP000056652};
RA   Brown N.M.;
RT   "The finished genome of an anatoxin-a-producing Anabaena isolate reveals
RT   extensive genome rearrangement.";
RL   Submitted (MAY-2015) 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; CP011456; ALB43253.1; -; Genomic_DNA.
DR   RefSeq; WP_053541054.1; NZ_CP011456.1.
DR   AlphaFoldDB; A0A0K2M5A3; -.
DR   STRING; 1647413.AA650_24895; -.
DR   KEGG; awa:AA650_24895; -.
DR   PATRIC; fig|1647413.5.peg.5859; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000056652; 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; cd05800; PGM_like2; 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   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   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}.
FT   DOMAIN          8..143
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          162..268
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          277..379
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          424..468
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   480 AA;  52522 MW;  4B5029D11665929A CRC64;
     MSVVTNPIKF GTDGWRGVIG EEFTFERLAL VATVAAKVLH NTYFSQVGSR TIIVGYDRRF
     MAEEFARVVA NAVTAVGFDV LFSETFAPTP AYSWAAKELK ALGALVVTAS HNPGAYLGLK
     VKSAFGGSVP PEVTQEIEAL LSEKVAPAAI PGKEETFDPW PSYCQALAAK VDIDKIKEAI
     ATGKLTIFVD VMHGAAAGGL ARLLGEQVKE INSDRDPLFE GGAPEPLPKY LSRLFTVMKT
     HRETHKTGLT VGLVFDGDCD RIAAVDQDAN FLSSQILIPI LIDHLTLRRN FQGEIVKTVS
     GSDLMPRVAA LHNLSIHETA VGYKYIADRM LTTQVLLGGE ESGGIGYGSH IPERDALLSA
     LYVLEAVVES GLDLGEYYRY LQQQTGFSSA YDRIDLPLAN MEVRGRLLQQ LQSQPLTEIA
     GKEVIGCQTI DGYKFRLADQ SWLMIRFSGT EPVLRLYCEA ATMEEVHQTL NWAKNWAESN
//
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