ID A0A0F0L6C6_9MICO Unreviewed; 547 AA.
AC A0A0F0L6C6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KJL27106.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KJL27106.1};
GN Name=pgm {ECO:0000313|EMBL:KJL27106.1};
GN ORFNames=RL72_00710 {ECO:0000313|EMBL:KJL27106.1};
OS Microbacterium azadirachtae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL27106.1, ECO:0000313|Proteomes:UP000033448};
RN [1] {ECO:0000313|EMBL:KJL27106.1, ECO:0000313|Proteomes:UP000033448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL27106.1,
RC ECO:0000313|Proteomes:UP000033448};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
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:KJL27106.1}.
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DR EMBL; JYIT01000058; KJL27106.1; -; Genomic_DNA.
DR RefSeq; WP_045249445.1; NZ_JYIT01000058.1.
DR AlphaFoldDB; A0A0F0L6C6; -.
DR PATRIC; fig|582680.7.peg.736; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000033448; 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; 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 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:KJL27106.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000033448}.
FT DOMAIN 38..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 322..440
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 492..541
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 547 AA; 58745 MW; 6D5EE7F245F29D93 CRC64;
MTSRAGLPAE ESDLIDVDEL IAAYYDRIPD PKISTERVVF GTSGHRGSSL SGSFNEQHIL
ATTQAIVDYR TAQGITGPLF LGRDTHALSR PAERSAIEVL VANDVDVLVD ARDAWVPTPA
LSHAILTYNR DRADDEPGRA DGIVVTPSHN PPRDGGFKYN PPHGGPADTD ATAWIANRAN
ELIEQGLEGV KRTRFADIDA DGLGTYDFRE AYVRDLPSII DIDAIKRAGV RIGADPLGGA
SVEYWALIAE MHGLDLTVVN PEVDPTWRFM TLDWDEKIRM DPSSPSAMAS LVAKKGDYDV
LTGNDADADR HGIVTPDAGL MNPNHYLAVA IDYLFSHREG WDRNAAIGKT LVSSMIIDRV
AESLGRRLLE VPVGFKWFVP GLLDGSVAFG GEESAGASFL RRDGSVWSTD KDGILLCLLA
AEIIAVTGKT PSERYRELEE AFGASAYQRV DAPATPEQKA TLGKLSPESV SATELAGEPI
TAKLSHAPGN GAAIGGLKVQ TEHAWFAARP SGTEDVYKLY AESLLGAEHL ARVQEEARAV
VSAALGA
//
