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Database: UniProt
Entry: B3QYJ2_CHLT3
LinkDB: B3QYJ2_CHLT3
Original site: B3QYJ2_CHLT3 
ID   B3QYJ2_CHLT3            Unreviewed;       480 AA.
AC   B3QYJ2;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:ACF13620.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:ACF13620.1};
GN   OrderedLocusNames=Ctha_1156 {ECO:0000313|EMBL:ACF13620.1};
OS   Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chloroherpetonaceae;
OC   Chloroherpeton.
OX   NCBI_TaxID=517418 {ECO:0000313|EMBL:ACF13620.1, ECO:0000313|Proteomes:UP000001208};
RN   [1] {ECO:0000313|EMBL:ACF13620.1, ECO:0000313|Proteomes:UP000001208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35110 / GB-78 {ECO:0000313|Proteomes:UP000001208};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
RL   Submitted (JUN-2008) 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; CP001100; ACF13620.1; -; Genomic_DNA.
DR   RefSeq; WP_012499704.1; NC_011026.1.
DR   AlphaFoldDB; B3QYJ2; -.
DR   STRING; 517418.Ctha_1156; -.
DR   KEGG; cts:Ctha_1156; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_7_1_10; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000001208; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004614; F:phosphoglucomutase 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:ACF13620.1};
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:UP000001208}.
FT   DOMAIN          3..136
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          169..273
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          278..390
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          424..473
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   480 AA;  53842 MW;  2B5B0C792F6EFE4C CRC64;
     MKIKFGTSGW RAIIADEFTY GNLTLVLEAI VRYLKEEKLG EKGIVIGRDT RFLGEEFSKL
     AAQTLAANGI KAFMCDRDVP TPVISYEITR RKAGGGLNFT ASHNPPDYQG IKFSTADGAP
     ALPEVTKKFE AYFSELYEAE QKNPTVRNYE SFDALKENGM IEIINPQETY LARLKELVDT
     DVIAKSGLKV VYDCMYGTAR DYTDKFLTDL GVDVEIMNNH RDVYFGGRPP EPSEPHIPEL
     IARVKERGAS GEFVIGIAND GDADRYAAID STGTYLQANQ LLAILFHYAL NHKPEWKGCV
     VRTLATSHLI DAIAKKEGVK LYDVPVGFKY IGEVMMREDM ILGGEESNGL SVFRHIPEKD
     GVLACLLFVE ITARTGKPLS EYLKSLYETY GHFYTMRENY RLSEEKKNAL LSSLQNETPT
     EIAGQKVVKV DRRDGVKMIC EDESWFLVRF SGTEPVVRFY AEAGSQERLN EILAFGKSLL
//
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