ID A0A0H5CNW4_9PSEU Unreviewed; 448 AA.
AC A0A0H5CNW4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:CRK59722.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:CRK59722.1};
OS Alloactinosynnema sp. L-07.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae.
OX NCBI_TaxID=1653480 {ECO:0000313|EMBL:CRK59722.1, ECO:0000313|Proteomes:UP000076116};
RN [1] {ECO:0000313|Proteomes:UP000076116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-07 {ECO:0000313|Proteomes:UP000076116};
RA Ramaraj T.;
RL Submitted (MAY-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}.
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DR EMBL; LN850107; CRK59722.1; -; Genomic_DNA.
DR RefSeq; WP_054051755.1; NZ_LN850107.1.
DR AlphaFoldDB; A0A0H5CNW4; -.
DR STRING; 1653480.gene:80948599; -.
DR KEGG; alo:CRK59722; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000076116; Chromosome i.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:CRK59722.1};
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:UP000076116}.
FT DOMAIN 7..133
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 151..250
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 261..364
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 369..447
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 448 AA; 47357 MW; 7F7097F00AB44092 CRC64;
MRDLSGVFKA YDIRGVVGEQ IDADLVRAIG AGFARLVGGP TIVVGYDMRD SSPGLADAFA
EGANGEGVDV VNIGLASTDM LYFASGSLNL PGAMFTASHN PAKYNGIKLC RAGAAPVGQD
SGLTDIQRDV ENETPGSGKT GSVERRDLLA EYAAYLNKLV DLSGSRPLKI VVDAGNGMGG
YTVPSVFADL PFEIIPMYFE LDGSFPNHEA NPLDPKNIVD LQAKVREVGA DAGLAFDGDA
DRCFVVDERG EPVSPSAVTA LVAVRELVKD PGGTIIHNLI TSHAVPEIVT EHGGKPVRTR
VGHSFIKEEM ARTGAIFGGE HSAHYYFRDF WKADTGMLAA LHVLAALGEQ DGPLSALTSE
YNRYAASGEI NSTVGDQADR LAAIKAEFGG RDGVELDELD GLTVQLPDGA WFNLRASNTE
PLLRLNIEAA DDAAVAALRD EVLAIVRA
//
