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GMHA_MYCTU
ID   GMHA_MYCTU              Reviewed;         196 AA.
AC   P9WGG1; L0T4C6; O53635; P0A604;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Phosphoheptose isomerase {ECO:0000255|HAMAP-Rule:MF_00067};
DE            EC=5.3.1.28 {ECO:0000255|HAMAP-Rule:MF_00067, ECO:0000269|PubMed:33257730};
DE   AltName: Full=Sedoheptulose 7-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00067, ECO:0000303|PubMed:33257730};
GN   Name=gmhA {ECO:0000255|HAMAP-Rule:MF_00067, ECO:0000303|PubMed:33257730};
GN   Synonyms=lpcA; OrderedLocusNames=Rv0113; ORFNames=MTV031.07;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.
RX   PubMed=12101286; DOI=10.1099/00221287-148-7-1979;
RA   Valvano M.A., Messner P., Kosma P.;
RT   "Novel pathways for biosynthesis of nucleotide-activated glycero-manno-
RT   heptose precursors of bacterial glycoproteins and cell surface
RT   polysaccharides.";
RL   Microbiology 148:1979-1989(2002).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP   PATHWAY, SUBUNIT, INTERACTION WITH HDDA AND GMHB, AND MUTAGENESIS OF
RP   ASN-53; SER-121; THR-122; SER-123; SER-126 AND GLN-173.
RC   STRAIN=H37Rv;
RX   PubMed=33257730; DOI=10.1038/s41598-020-77230-8;
RA   Karan S., Pratap B., Yadav S.P., Ashish F., Saxena A.K.;
RT   "Structural and functional characterization of M. tuberculosis
RT   sedoheptulose-7-phosphate isomerase, a critical enzyme involved in
RT   lipopolysaccharide biosynthetic pathway.";
RL   Sci. Rep. 10:20813-20813(2020).
CC   -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in
CC       D-glycero-D-manno-heptose 7-phosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_00067, ECO:0000269|PubMed:33257730}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-
CC         heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate;
CC         Xref=Rhea:RHEA:27489, ChEBI:CHEBI:57483, ChEBI:CHEBI:60203,
CC         ChEBI:CHEBI:60204; EC=5.3.1.28; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00067, ECO:0000269|PubMed:33257730};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00067,
CC         ECO:0000305|PubMed:33257730};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00067};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.31 mM for D-sedoheptulose 7-phosphate
CC         {ECO:0000269|PubMed:33257730};
CC         Note=kcat is 0.45 sec(-1). {ECO:0000269|PubMed:33257730};
CC   -!- PATHWAY: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-
CC       phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and
CC       D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-
CC       phosphate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00067}.
CC   -!- PATHWAY: Lipopolysaccharide biosynthesis; LPS oligosaccharide
CC       biosynthesis. {ECO:0000305|PubMed:33257730}.
CC   -!- SUBUNIT: Homotetramer (PubMed:33257730). Interacts wit HddA and GmhB
CC       (PubMed:33257730). {ECO:0000269|PubMed:33257730}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00067}.
CC   -!- MISCELLANEOUS: The reaction produces a racemic mixture of D-glycero-
CC       alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00067}.
CC   -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00067}.
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DR   EMBL; AL123456; CCP42838.1; -; Genomic_DNA.
DR   PIR; D70840; D70840.
DR   RefSeq; NP_214627.1; NC_000962.3.
DR   RefSeq; WP_003400839.1; NZ_NVQJ01000062.1.
DR   AlphaFoldDB; P9WGG1; -.
DR   SMR; P9WGG1; -.
DR   STRING; 83332.Rv0113; -.
DR   PaxDb; P9WGG1; -.
DR   DNASU; 886905; -.
DR   GeneID; 45424078; -.
DR   GeneID; 886905; -.
DR   KEGG; mtu:Rv0113; -.
DR   TubercuList; Rv0113; -.
DR   eggNOG; COG0279; Bacteria.
DR   OMA; DVHICVP; -.
DR   PhylomeDB; P9WGG1; -.
DR   BRENDA; 5.3.1.28; 3445.
DR   UniPathway; UPA00041; UER00436.
DR   UniPathway; UPA00301; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0008968; F:D-sedoheptulose 7-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:2001061; P:D-glycero-D-manno-heptose 7-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05006; SIS_GmhA; 1.
DR   HAMAP; MF_00067; GmhA; 1.
DR   InterPro; IPR035461; GmhA/DiaA.
DR   InterPro; IPR004515; Phosphoheptose_Isoase.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   Pfam; PF13580; SIS_2; 1.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Isomerase; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..196
FT                   /note="Phosphoheptose isomerase"
FT                   /id="PRO_0000136536"
FT   DOMAIN          38..196
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         53..55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         95..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         121..123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   MUTAGEN         53
FT                   /note="N->G: 3.5-fold decrease in catalytic efficiency."
FT                   /evidence="ECO:0000269|PubMed:33257730"
FT   MUTAGEN         121
FT                   /note="S->G: 3.1-fold decrease in catalytic efficiency."
FT                   /evidence="ECO:0000269|PubMed:33257730"
FT   MUTAGEN         122
FT                   /note="T->A: 14.5-fold decrease in catalytic efficiency."
FT                   /evidence="ECO:0000269|PubMed:33257730"
FT   MUTAGEN         123
FT                   /note="S->A: 4.4-fold decrease in catalytic efficiency."
FT                   /evidence="ECO:0000269|PubMed:33257730"
FT   MUTAGEN         126
FT                   /note="S->A: 6.6-fold decrease in catalytic efficiency."
FT                   /evidence="ECO:0000269|PubMed:33257730"
FT   MUTAGEN         173
FT                   /note="Q->A: 24-fold decrease in catalytic efficiency."
FT                   /evidence="ECO:0000269|PubMed:33257730"
SQ   SEQUENCE   196 AA;  20923 MW;  0F05EB968F1189CB CRC64;
     MCTARTAEEI FVETIAVKTR ILNDRVLLEA ARAIGDRLIA GYRAGARVFM CGNGGSAADA
     QHFAAELTGH LIFDRPPLGA EALHANSSHL TAVANDYDYD TVFARALEGS ARPGDTLFAI
     STSGNSMSVL RAAKTARELG VTVVAMTGES GGQLAEFADF LINVPSRDTG RIQESHIVFI
     HAISEHVEHA LFAPRQ
 
 
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