P0A604 (GMHA_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoheptose isomerase
EC=5.3.1.28

Alternative name(s):
Sedoheptulose 7-phosphate isomerase

Gene names

Name:	gmhA
Synonyms:	lpcA
Ordered Locus Names:	Rv0113, MT0122
ORF Names:	MTV031.07

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	196 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate By similarity. HAMAP MF_00067
Catalytic activity	D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate. HAMAP MF_00067
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00067
Pathway	Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1. HAMAP MF_00067
Subcellular location	Cytoplasm By similarity HAMAP MF_00067.
Miscellaneous	The reaction produces a racemic mixture of D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate By similarity. HAMAP MF_00067
Sequence similarities	Belongs to the SIS family. GmhA subfamily. Contains 1 SIS domain.
Sequence caution	The sequence AAK44345.1 differs from that shown. Reason: Frameshift at position 179. Fuses together gmhA and gmhB.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	D-sedoheptulose 7-phosphate isomerase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sugar binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 196	196	Phosphoheptose isomerase HAMAP MF_00067		PRO_0000136536
Regions
	Domain	38 – 196	159	SIS
	Region	53 – 55	3	Substrate binding By similarity
	Region	95 – 96	2	Substrate binding By similarity
	Region	121 – 123	3	Substrate binding By similarity
Sites
	Metal binding	62	1	Zinc By similarity
	Metal binding	66	1	Zinc By similarity
	Metal binding	173	1	Zinc By similarity
	Metal binding	181	1	Zinc By similarity
	Binding site	66	1	Substrate By similarity
	Binding site	126	1	Substrate By similarity
	Binding site	173	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A604 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 0F05EB968F1189CB	FASTA	196	20,923
	10 20 30 40 50 60 MCTARTAEEI FVETIAVKTR ILNDRVLLEA ARAIGDRLIA GYRAGARVFM CGNGGSAADA 70 80 90 100 110 120 QHFAAELTGH LIFDRPPLGA EALHANSSHL TAVANDYDYD TVFARALEGS ARPGDTLFAI 130 140 150 160 170 180 STSGNSMSVL RAAKTARELG VTVVAMTGES GGQLAEFADF LINVPSRDTG RIQESHIVFI 190 HAISEHVEHA LFAPRQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides." Valvano M.A., Messner P., Kosma P. Microbiology 148:1979-1989(2002) [PubMed: 12101286] [Abstract] Cited for: BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842572 Genomic DNA. Translation: CAA17307.1. AE000516 Genomic DNA. Translation: AAK44345.1. Frameshift.
PIR	D70840.
RefSeq	NP_214627.1. NC_000962.2.
3D structure databases
ProteinModelPortal	P0A604.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000002695; EBMYCP00000002695; EBMYCG00000002693. EBMYCT00000072732; EBMYCP00000070791; EBMYCG00000072727.
GeneID	886905.
GenomeReviews	Gene locus MT0122 in contig AE000516_GR. Gene locus Rv0113 in contig AL123456_GR.
KEGG	mtc:MT0122. mtu:Rv0113.
PATRIC	18148749. VBIMycTub87468_0127.
TIGR	MT0122.
Organism-specific databases
TubercuList	Rv0113.
Phylogenomic databases
GeneTree	EBGT00050000016043. EBGT00050000016047.
HOGENOM	HBG671955.
OMA	HITIIHI.
PhylomeDB	P0A604.
Family and domain databases
HAMAP	MF_00067. GmhA. [Tree]
InterPro	IPR020620. Phosphoheptose_isomerase. IPR001347. SIS. [Graphical view]
KO	K03271.
Pfam	PF01380. SIS. 1 hit. [Graphical view]
PROSITE	PS51464. SIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GMHA_MYCTU

Accession

Primary (citable) accession number: P0A604
Secondary accession number(s): O53635

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program