ID A0A1I1DLZ6_9ACTN Unreviewed; 461 AA.
AC A0A1I1DLZ6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:SFB75392.1};
GN ORFNames=SAMN04487968_101323 {ECO:0000313|EMBL:SFB75392.1};
OS Nocardioides terrae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=574651 {ECO:0000313|EMBL:SFB75392.1, ECO:0000313|Proteomes:UP000198832};
RN [1] {ECO:0000313|EMBL:SFB75392.1, ECO:0000313|Proteomes:UP000198832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7056 {ECO:0000313|EMBL:SFB75392.1,
RC ECO:0000313|Proteomes:UP000198832};
RA de Groot N.N.;
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; FOLB01000001; SFB75392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1DLZ6; -.
DR STRING; 574651.SAMN04487968_101323; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000198832; 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:UP000198832}.
FT DOMAIN 13..138
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 162..262
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 272..376
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 381..458
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 461 AA; 49230 MW; 5013FAA9FA1795EA CRC64;
MASSLDPANV GAVFKAYDVR GTVPDQVDED LARATGRAFV RVLDTPEDPV RRIVIGHDMR
PSSPSLARAY AEGANQAGAD VVMIGLASTD QLYFASGHLG LPGVMFTASH NPAQYNGIKQ
CRPFAAPVGM ESGLAEIRDL VLQGSPLEQE HSGTVEEQDV LEAYADHLLS LAPVSGRPLT
VVADAGNGMA GHTAPAVFAR LPGIELVPMY FELDGTFPHH EANPIEPENL VDLQAKVRET
GADVGLAFDG DADRCFLVDE RGQLVSPSTL TALIAARELA KAPGSAVIHN LITSRAVPQI
VSELGGRPVR TRVGHSFIKA RMAETDAVFG GEHSGHFYFR DFWRADSGML AALHALAALA
EADVPLSELL APYERYPLSG EINSTVADQQ AVVAEIEATY GGRDGAALDR LDGLTVSTDD
WSFNVRASNT EPLLRLNVEG KDTATMEHLR DEVLAIIRKD A
//
