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Database: UniProt
Entry: A0A0K9XNP1_9ACTN
LinkDB: A0A0K9XNP1_9ACTN
Original site: A0A0K9XNP1_9ACTN 
ID   A0A0K9XNP1_9ACTN        Unreviewed;       452 AA.
AC   A0A0K9XNP1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:KNB54322.1};
GN   Name=manB {ECO:0000313|EMBL:KNB54322.1};
GN   ORFNames=AC230_00045 {ECO:0000313|EMBL:KNB54322.1};
OS   Streptomyces caatingaensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1678637 {ECO:0000313|EMBL:KNB54322.1, ECO:0000313|Proteomes:UP000037288};
RN   [1] {ECO:0000313|Proteomes:UP000037288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMAA 1322 {ECO:0000313|Proteomes:UP000037288};
RA   Santos S.N., Gacesa R., Taketani R.G., Long P.F., Melo I.S.;
RT   "Draft genome sequence of Streptomyces sp. CMAA 1322, a bacterium isolated
RT   from Caatinga biome, from dry forest semiarid of Brazil.";
RL   Submitted (JUL-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNB54322.1}.
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DR   EMBL; LFXA01000001; KNB54322.1; -; Genomic_DNA.
DR   RefSeq; WP_049713837.1; NZ_LFXA01000001.1.
DR   AlphaFoldDB; A0A0K9XNP1; -.
DR   STRING; 1678637.AC230_00045; -.
DR   PATRIC; fig|1678637.3.peg.9; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000037288; 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:UP000037288}.
FT   DOMAIN          6..132
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          156..255
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          263..369
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          374..451
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   452 AA;  47957 MW;  BF5BB593F487757A CRC64;
     MADLSQLVKA YDVRGVVPDQ WDERLARLFG AAFVEVTGAG AVVVGHDMRP SSPGLSRAFA
     EGAADRGADV TEIGLCSTDQ LYFASGHLGL PGAMFTASHN PAQYNGIKMC RAGAAPVGQD
     TGLAEIRALV EGWTESGAPA AVARPGTLER RDTLADYAAH LRSLVDLTGI RRLKAVVDAG
     NGMGGHTVPT VLDGLPIDVV ALYFELDGTF PNHEANPLDP KNLVDLQAKV RETGADIGLA
     FDGDADRCFV IDERGEPVSP SAITALVAAR ELAKHPGGTV IHNLITSHSV PEVVREHGGE
     PVRTRVGHSF IKQEMARTGA IFGGEHSAHY YFRDFWNADT GMLAALHVLA ALGEQAGPLS
     ELVRAYDRYA ASGEINSTVA DQPGRMAAVK AAYAGGENVT VDELDGLTVT TPDWWFNLRA
     SNTEPLLRLN VEARDAATVA RVRDEVLAVV RA
//
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