PGMUT_SULTO
ID PGMUT_SULTO Reviewed; 455 AA.
AC Q976E4;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Phosphoglucosamine/phosphogalactosamine mutase {ECO:0000305};
DE EC=5.4.2.10 {ECO:0000269|PubMed:29507091};
DE EC=5.4.2.13 {ECO:0000269|PubMed:29507091};
DE AltName: Full=PGlcNM {ECO:0000303|PubMed:29507091};
GN OrderedLocusNames=STK_02420 {ECO:0000312|EMBL:BAB65203.1};
GN ORFNames=ST0242 {ECO:0000303|PubMed:29507091};
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=29507091; DOI=10.1128/jb.00048-18;
RA Dadashipour M., Iwamoto M., Hossain M.M., Akutsu J.I., Zhang Z.,
RA Kawarabayasi Y.;
RT "Identification of a direct biosynthetic pathway for UDP-N-
RT acetylgalactosamine from glucosamine-6-phosphate in thermophilic
RT crenarchaeon Sulfolobus tokodaii.";
RL J. Bacteriol. 200:E00048-E00048(2018).
RN [3] {ECO:0007744|PDB:2F7L}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS).
RA Kawamura T., Sakai N., Akutsu J., Zhang Z., Watanabe N., Kawarabayashi Y.,
RA Tanaka I.;
RT "Crystal structure of Sulfolobus tokodaii
RT phosphomannomutase/phosphoglucomutase.";
RL Submitted (DEC-2005) to the PDB data bank.
CC -!- FUNCTION: Involved in the synthesis of UDP-N-acetylglucosamine (UDP-
CC GlcNAc) and UDP-N-acetylgalactosamine (UDP-GalNAc). Catalyzes the
CC conversion of glucosamine-6-phosphate to glucosamine-1-phosphate and of
CC galactosamine-6-phosphate to galactosamine-1-phosphate.
CC {ECO:0000269|PubMed:29507091}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate;
CC Xref=Rhea:RHEA:23424, ChEBI:CHEBI:58516, ChEBI:CHEBI:58725;
CC EC=5.4.2.10; Evidence={ECO:0000269|PubMed:29507091};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactosamine 6-phosphate = alpha-D-galactosamine 1-
CC phosphate; Xref=Rhea:RHEA:46048, ChEBI:CHEBI:71674,
CC ChEBI:CHEBI:142399; EC=5.4.2.13;
CC Evidence={ECO:0000269|PubMed:29507091};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00949};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00949};
CC -!- PTM: Activated by phosphorylation. {ECO:0000250|UniProtKB:P31120}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; BA000023; BAB65203.1; -; Genomic_DNA.
DR RefSeq; WP_010978186.1; NC_003106.2.
DR PDB; 2F7L; X-ray; 2.80 A; A/B=1-455.
DR PDBsum; 2F7L; -.
DR AlphaFoldDB; Q976E4; -.
DR SMR; Q976E4; -.
DR STRING; 273063.STK_02420; -.
DR EnsemblBacteria; BAB65203; BAB65203; STK_02420.
DR GeneID; 42799725; -.
DR KEGG; sto:STK_02420; -.
DR PATRIC; fig|273063.9.peg.288; -.
DR eggNOG; arCOG00767; Archaea.
DR OMA; PHNPEPL; -.
DR OrthoDB; 58941at2157; -.
DR BioCyc; MetaCyc:MON-20593; -.
DR BRENDA; 5.4.2.13; 15396.
DR EvolutionaryTrace; Q976E4; -.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03087; PGM_like1; 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 InterPro; IPR024086; GlmM_arc-type.
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; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR TIGRFAMs; TIGR03990; Arch_GlmM; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Magnesium; Metal-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..455
FT /note="Phosphoglucosamine/phosphogalactosamine mutase"
FT /id="PRO_0000448050"
FT ACT_SITE 97
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P31120"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31120"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:2F7L"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:2F7L"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:2F7L"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 259..272
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 290..296
FT /evidence="ECO:0007829|PDB:2F7L"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:2F7L"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 342..356
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 360..365
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 371..378
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 385..396
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 406..413
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 416..422
FT /evidence="ECO:0007829|PDB:2F7L"
FT STRAND 424..437
FT /evidence="ECO:0007829|PDB:2F7L"
FT HELIX 438..452
FT /evidence="ECO:0007829|PDB:2F7L"
SQ SEQUENCE 455 AA; 50103 MW; D94783475A8D480E CRC64;
MGKLFGTDGV RGIVNKELTP ELVLKLSKAI GTFFGKNSKI LVGRDVRAGG DMLVKIVEGG
LLSVGVEVYD GGMAPTPALQ YAVKTLGYDG GVVITASHNP APYNGIKVVD KDGIEIRREK
ENEIEDLFFT ERFNTIEWSS LTTEVKREDR VISTYVNGIL SHVDIEKIKK KNYKVLIDPA
NSVGALSTPL VARALGCKIY TINGNLDPLF SARQPEPTFD SLKETAEVVK TLKVDLGVAH
DGDADRAIFI DSEGRVQWGD RSGTLLSYWA SVKNPKAIKK IVTAVSSSSL VEEYLSKYNI
QVDWTKVGSV DIAHKVADEN ALAGFEENGG FMYPPHQYVR DGAMSFALML ELLANENVSS
AELFDRLPKY YLVKTKVDLK PGLMVEEIYK KILEVYSTSS VKAITIDGVK IIGKDFWFLV
RKSGTEPIIR IMAEAKDENV ANNLVNELKK IVEGK
