ID   A0A1I1A8Q3_9PSEU        Unreviewed;       557 AA.
AC   A0A1I1A8Q3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:SFB33806.1};
GN   ORFNames=SAMN05216266_108248 {ECO:0000313|EMBL:SFB33806.1};
OS   Amycolatopsis marina.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=490629 {ECO:0000313|EMBL:SFB33806.1, ECO:0000313|Proteomes:UP000243799};
RN   [1] {ECO:0000313|Proteomes:UP000243799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3568 {ECO:0000313|Proteomes:UP000243799};
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, ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; FOKG01000008; SFB33806.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1A8Q3; -.
DR   STRING; 490629.SAMN05216266_108248; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000243799; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05799; PGM2; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
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   PRINTS; PR00509; PGMPMM.
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};
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:UP000243799}.
FT   DOMAIN          58..192
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          216..312
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          326..436
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          454..526
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   557 AA;  58077 MW;  9E26981464E51E73 CRC64;
     MTTPARLTPE LRDSAFRWIA DDADPEARTE LQAVLARAMG GEEAAVAELT DRMAGPLEFG
     TAGLRGPVRA GPNGMNLAVV IRTTAGVAAW LDRHGHTGAT VVVGRDARHG SEAFAAAAAD
     VLTAAGFDVR VLPRPLPTPV LAFAARHFGA AAAIQITASH NPPADNGYKL YDDTAVQIVP
     PADGEIEAAI EAVPAAVSVP RAPGATPLGE DVVRAYLSRV AALPAGQHRD LRVAATALHG
     VGADVLRAAL HEAGFTDVHL VAEQAAPDPD FPTVSFPNPE EPGVTDLLLA LAVEVAADIA
     IALDPDADRC ALGVADAHGA WRMLRGDESG VLLGEHILST LDKTVVPDPL VATTIVSSSM
     LAGIARAHGA RFAQTLTGFK WLARAGTGLV FAYEEALGLC VNPGFVRDKD GIAAAVLACD
     LAATLKAQGQ SLLDALDTLA ARHGVHLTDQ ISLRVTDLDR IGRLMAELRA APPTELAGQP
     VTSEDLLPEA DVLRLNGTGA RVVIRPSGTE PKLKAYLEVT EPATAETGLA PARKRANERL
     TTLRAEVHTL FGMHARR
//