ID A0A0D8ZR31_9CYAN Unreviewed; 479 AA.
AC A0A0D8ZR31;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:KJH71258.1};
GN ORFNames=UH38_13275 {ECO:0000313|EMBL:KJH71258.1};
OS Aliterella atlantica CENA595.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC Aliterellaceae; Aliterella.
OX NCBI_TaxID=1618023 {ECO:0000313|EMBL:KJH71258.1, ECO:0000313|Proteomes:UP000032452};
RN [1] {ECO:0000313|EMBL:KJH71258.1, ECO:0000313|Proteomes:UP000032452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CENA595 {ECO:0000313|EMBL:KJH71258.1,
RC ECO:0000313|Proteomes:UP000032452};
RA Rigonato J., Alvarenga D.O., Branco L.H., Varani A.M., Brandini F.P.,
RA Fiore M.F.;
RT "Draft genome of a novel marine cyanobacterium (Chroococcales) isolated
RT from South Atlantic Ocean.";
RL Submitted (FEB-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}.
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:KJH71258.1}.
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DR EMBL; JYON01000013; KJH71258.1; -; Genomic_DNA.
DR RefSeq; WP_045055148.1; NZ_JYON01000013.1.
DR AlphaFoldDB; A0A0D8ZR31; -.
DR STRING; 1618023.UH38_13275; -.
DR PATRIC; fig|1618023.3.peg.4684; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000032452; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProt.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000032452}.
FT DOMAIN 8..145
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 162..270
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 278..382
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 417..470
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 479 AA; 52188 MW; 36D903A5698F688C CRC64;
MPVAAKEIKF GTDGWRGIIG DDFTFDRLTL VAPIATRVLL ETYGDTVNNK KIIVGYDRRF
MAETFAEKTA AAVMAAGFDV MLADSYASTP AFSWAVKHHN ALGALVITAS HNPGDYLGLK
VKGAFGGSVP PEVTQKIEGL LQSESLAATT QGTLQKFQPW ANYCENLRQK VDISQICDRI
NAGKLTVFVD VMHGAAAGGM AQILGVPVQE INSDRDPLFE GGAPEPLPRY LSKLFSQIRS
HRRSQASDAL AVGFVFDGDG DRIAAVDGQG NFLSSQILIP ILIEHLAARR GLTGEIVRTV
SGSDLISLVA QMYNLPIYET PVGYKYIADR MLASNVLLGG EESGGIGYAD YIPERDGLLS
ALYVLEAIAQ SGLDLSELYS SLQAKTNFHS AYDRIDLPLA SMDVRSRLLQ QLQTQPLKEI
AGKQVVDCIS IDGYKFRLAD NSWLMIRFSG TEPVLRLYCE AADLEQVHQT LAWAKEWAA
//
