ID A0A0C1JWX5_9BACT Unreviewed; 554 AA.
AC A0A0C1JWX5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KIC74941.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KIC74941.1};
GN Name=celB {ECO:0000313|EMBL:KIC74941.1};
GN ORFNames=DB41_IB00740 {ECO:0000313|EMBL:KIC74941.1};
OS Neochlamydia sp. TUME1.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Neochlamydia.
OX NCBI_TaxID=1478174 {ECO:0000313|EMBL:KIC74941.1, ECO:0000313|Proteomes:UP000031320};
RN [1] {ECO:0000313|EMBL:KIC74941.1, ECO:0000313|Proteomes:UP000031320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUME1 {ECO:0000313|EMBL:KIC74941.1,
RC ECO:0000313|Proteomes:UP000031320};
RX PubMed=25069652; DOI=10.1093/molbev/msu227;
RA Domman D., Collingro A., Lagkouvardos I., Gehre L., Weinmaier T.,
RA Rattei T., Subtil A., Horn M.;
RT "Massive expansion of Ubiquitination-related gene families within the
RT Chlamydiae.";
RL Mol. Biol. Evol. 31:2890-2904(2014).
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:KIC74941.1}.
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DR EMBL; JRXI01000136; KIC74941.1; -; Genomic_DNA.
DR RefSeq; WP_039385759.1; NZ_JRXI01000136.1.
DR AlphaFoldDB; A0A0C1JWX5; -.
DR PATRIC; fig|1478174.3.peg.1510; -.
DR Proteomes; UP000031320; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05801; PGM_like3; 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 InterPro; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
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, ECO:0000313|EMBL:KIC74941.1};
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 41..181
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..316
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 323..441
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 486..536
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 554 AA; 61292 MW; 5A16C450B75A6848 CRC64;
MRVSPLAGKI SPSDKLVNIP QLITAYYAEK PDPLDTAQQV AFGTSGHRGS ALQKSFNEHH
ILAISQAICQ YRKQQGIDGP LFLGMDTHAL SKPALMSAIE VLAANGIEIL LAEGEEYTPT
PVISHAIVSY NRHRTKNLAD GIVITPSHNP PSQGGIKYNP PSGGPADLHI TQWIETKANE
LMRHELRDLK RIPYEKALNL STTKRYNYLE AYVSDLKNVI NMEIIQKSQI KLGVDPLGGA
GIHYWEPIAE RYKLNLTLVN KAIDPTFQFM TLDWDGQIRM DPSSAYAMQG LITLKNRFDI
AFACDTDHDR HGIVTKSSGL LPPNHYLSAA IFYLFQHRPL WSPETAIGKT LVSSQMIDRV
ATQLNRKIYE VPVGFKWFVD GLLNESLSFC GEESAGASFA RLDGKTWTTD KDGIILSLLA
AEMTAQQGKD PGEIYQDLTR EFGNPAYDRV EAPASLKQRQ ILKNFSALQI QAKEIAGEAI
QGIFTHAAGN NAAIGGVKVI TENGWFAARP SGTEDIYKIY GESFRGQEHL EQILNEAQSI
VGKAFEEAYL LKTP
//
