ID W5WSY0_9PSEU Unreviewed; 449 AA.
AC W5WSY0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Phosphomannomutase {ECO:0008006|Google:ProtNLM};
GN ORFNames=KALB_7907 {ECO:0000313|EMBL:AHI01265.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHI01265.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHI01265.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHI01265.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
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; CP007155; AHI01265.1; -; Genomic_DNA.
DR RefSeq; WP_025361081.1; NZ_CP007155.1.
DR AlphaFoldDB; W5WSY0; -.
DR STRING; 1449976.KALB_7907; -.
DR KEGG; kal:KALB_7907; -.
DR PATRIC; fig|1449976.3.peg.7942; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_9_2_11; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000019225; Chromosome.
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:UP000019225}.
FT DOMAIN 8..121
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 152..251
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 259..365
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 370..448
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 449 AA; 47424 MW; 82B4E1C8EB172E00 CRC64;
MPDLSAVVKA YDIRGVVGEQ LDADVVRALG AAFARLVGGP SVVIGHDMRD SSPELSAAFA
EGVTGQGVDV VSIGLASTDM LYFASGRLQL PGAMFTASHN PAKYNGIKLC RAGAAPVGQD
SGLAEIRGWA EQGVPAHEGR TGIVSERDML AEYAAYLREL VDLSGIRPLK VVVDAGNGMG
GHTVPSVFAG LPIELVPMYF ELDGTFPNHE ANPLDPANLV DLQAKVREVG ADAGLAFDGD
ADRCFVVDAD GEPVSPSAVT ALVATRELAK EPGATIIHNL ITSRAVPEIV EEHGGKPVRT
RVGHSFIKEQ MAETGAIFGG EHSAHYYFRD FWRADTGMLA ALHVLAALGE QDRPLAELTS
VFSRYAASGE INSTVADQAA STEAVRAEFG AREGVTFDEL DGLTVDLGDG RWFNLRASNT
EPLLRLNVEA PDEQAVAALR DEVLAIVRG
//
