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 27-MAR-2024, entry version 43.
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; Actinomycetota; Actinomycetes; Mycobacteriales; 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; 83332-Rv0113; -.
DR DNASU; 886905; -.
DR GeneID; 45424078; -.
DR GeneID; 886905; -.
DR KEGG; mtu:Rv0113; -.
DR TubercuList; Rv0113; -.
DR eggNOG; COG0279; Bacteria.
DR InParanoid; P9WGG1; -.
DR OrthoDB; 9810929at2; -.
DR PhylomeDB; P9WGG1; -.
DR BRENDA; 5.3.1.28; 3445.
DR SABIO-RK; P9WGG1; -.
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 PANTHER; PTHR30390:SF6; DNAA INITIATOR-ASSOCIATING PROTEIN DIAA; 1.
DR PANTHER; PTHR30390; SEDOHEPTULOSE 7-PHOSPHATE ISOMERASE / DNAA INITIATOR-ASSOCIATING FACTOR FOR REPLICATION INITIATION; 1.
DR Pfam; PF13580; SIS_2; 1.
DR SUPFAM; SSF53697; SIS domain; 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
//
