ID K9VZ69_9CYAN Unreviewed; 479 AA.
AC K9VZ69;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:AFZ12839.1};
DE EC=5.4.2.10 {ECO:0000313|EMBL:AFZ12839.1};
GN ORFNames=Cri9333_1959 {ECO:0000313|EMBL:AFZ12839.1};
OS Crinalium epipsammum PCC 9333.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC Crinalium.
OX NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ12839.1, ECO:0000313|Proteomes:UP000010472};
RN [1] {ECO:0000313|EMBL:AFZ12839.1, ECO:0000313|Proteomes:UP000010472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ12839.1,
RC ECO:0000313|Proteomes:UP000010472};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Crinalium epipsammum PCC 9333.";
RL Submitted (JUN-2012) 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}.
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DR EMBL; CP003620; AFZ12839.1; -; Genomic_DNA.
DR RefSeq; WP_015202955.1; NC_019753.1.
DR AlphaFoldDB; K9VZ69; -.
DR STRING; 1173022.Cri9333_1959; -.
DR KEGG; cep:Cri9333_1959; -.
DR PATRIC; fig|1173022.3.peg.2112; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_1_3; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000010472; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-EC.
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; 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; 2.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AFZ12839.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010472}.
FT DOMAIN 10..144
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 164..264
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 269..377
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 411..469
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 479 AA; 52171 MW; DF0495D07A9520C5 CRC64;
MSTASSSQQI KFGTDGWRGI IADDFTFANV CKVTRAIANY LETAYSKDRP VLIAYDTRFL
ADQFAHTAAS VLADLGWTVL VTDRDCPTPV IAYNARLLNS AGALMFTASH NPAPYCGIKY
IPDYAGPATP QITDTIVANI EGATDQPPSG SNLDKISTFD PKPEYLKFIY TLIDVERIKS
AKLKVKYDAL YSTSRGYLDT VLEHCGCETE SFHTYRDVLF GGGMPEPKGE QLIELVEAVK
KDHADIGLAT DGDSDRFGIV DEQGNVLTPN TVLLLLARHL SKNKGKTGAI VRTVATTHLL
DNLAGKYGLQ IYETAVGFKY IGEKMRETQV LIGGEESGGL SVIGHIPEKD GILADMLVAE
AIAYEGKPLS QLVAEAIAEA DGPLYNNRLD LHLEEAHKAA VLDSFTKNPP AEVSGIKIKE
VGRKDGIKLY LEEGSWVLLR PSGTEPLMRV YMETNTPEKL GQIAQYMESM IADLKPVGV
//
