ID A0A1I2HJ61_9MICO Unreviewed; 489 AA.
AC A0A1I2HJ61;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:SFF28907.1};
GN ORFNames=SAMN04488035_2334 {ECO:0000313|EMBL:SFF28907.1};
OS Flavimobilis marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae;
OC Flavimobilis.
OX NCBI_TaxID=285351 {ECO:0000313|EMBL:SFF28907.1, ECO:0000313|Proteomes:UP000198520};
RN [1] {ECO:0000313|Proteomes:UP000198520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19083 {ECO:0000313|Proteomes:UP000198520};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FONZ01000004; SFF28907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2HJ61; -.
DR STRING; 285351.SAMN04488035_2334; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000198520; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
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:UP000198520}.
FT DOMAIN 13..132
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 169..274
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 302..394
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 399..483
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 489 AA; 51659 MW; 0A9D99CDD0E6DCD0 CRC64;
MSTDIVDLSG IIKAYDVRGV VPDTFDATIA RAIGAAFATV VVLPEAAPGS RPTAVVGHDM
RDTGPELVAA FAAGLTAAGV DVVSIGLCST DGLYHASGAH DVPGAMFTAS HNPAEYNGIK
LCRKGARPVG QDSGLAEVRD LAGAYLGGAQ QPVTATAPGS LTERSTLSDY ASFLRSLVDL
RGIRPLKVVV DAGNGMGGYT VPAVLGSAAG LDALPLDVVP LYFELDGTFP NHEANPLEPE
NLRDLQAAVV EHGADLGLAF DGDADRCFVI DERGEPVSPS AITALVGLRE VARERALDDS
RTPVVIHNLI TSRVVPDLLG AAGARTVRTR VGHSFIKAQM AEQDAVFGGE HSAHYYFRDF
FFADTGMLAA MHVLAALGEQ PHPLSALAEM YEPYFASGEI NSRTADVPAA RARVVEAYVT
QQGAGPVVVD ELDGLTVSHW DETPQWWFNL RASNTEPLLR LNVEAADEDI MVKVRDDVLA
LVRAEDEDA
//
