ID G7M2I8_9CLOT Unreviewed; 503 AA.
AC G7M2I8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I {ECO:0000313|EMBL:EHI99121.1};
GN ORFNames=CDLVIII_2478 {ECO:0000313|EMBL:EHI99121.1};
OS Clostridium sp. DL-VIII.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHI99121.1, ECO:0000313|Proteomes:UP000005106};
RN [1] {ECO:0000313|EMBL:EHI99121.1, ECO:0000313|Proteomes:UP000005106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHI99121.1,
RC ECO:0000313|Proteomes:UP000005106};
RX PubMed=23929491;
RA Taghavi S., Izquierdo J.A., van der Lelie D.;
RT "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL Genome Announc. 1:e00605-e00613(2013).
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; CM001240; EHI99121.1; -; Genomic_DNA.
DR RefSeq; WP_009169793.1; NZ_CM001240.1.
DR AlphaFoldDB; G7M2I8; -.
DR STRING; 641107.CDLVIII_2478; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_6_0_9; -.
DR Proteomes; UP000005106; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03089; PMM_PGM; 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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005106}.
FT DOMAIN 9..152
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 192..277
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 282..395
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 503 AA; 55293 MW; 11DB5D32DDC14AB7 CRC64;
MLVDYEKLQN GSDIRGIAIG GAGKKVNLVP QVAKFIAYGF VRMLENKINA KAENLKIAVG
IDSRLSGPDL KAAVIEELTD LGCSVYDCSM ATTPAMFMTT VLENYKCDGS IMITASHLPY
YYNGLKFFTK EGGCEKEDIQ NILSIASKEE SYNSANLGEV SKVDLIDEYS KILAGMIRRG
ADAKVNYDKP LAGFKIVVDA GNGAGGFFAY KVLKTLGADI TGSQFTDPDG TFPNHIPNPE
NKEAMESIRN AVLENRADLG IIFDTDVDRA AIVDSHGMEI NKNALIALIS SIVLEEHPNS
IIVTDSITST GLGEFINKSG GIHHRFKRGY RNVINEAVRL NNEGKESDLA IETSGHAALK
ENYFLDDGAY LIAKILIKMA KLNAEGKRIE SLIKDLKMPC ESTDFRIEIR KENFREYGSR
IIGDLESYAN RTGFSIVPNN YEGIRVACNK ANGDGWFLLR LSLHEPVLAL NIESDTKGGT
QIIIDKLLPF LEKYDQLEIS SIK
//
