6PGL_MYCTU
ID 6PGL_MYCTU Reviewed; 247 AA.
AC P9WQP5; L0T9F2; O06814; P63338;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=6-phosphogluconolactonase;
DE Short=6PGL;
DE EC=3.1.1.31;
GN Name=pgl; Synonyms=devB; OrderedLocusNames=Rv1445c; ORFNames=MTCY493.09;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
CC + H(+); Xref=Rhea:RHEA:12556, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57955, ChEBI:CHEBI:58759; EC=3.1.1.31;
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 2/3.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. 6-phosphogluconolactonase subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP44204.1; -; Genomic_DNA.
DR PIR; H70916; H70916.
DR RefSeq; NP_215961.1; NC_000962.3.
DR RefSeq; WP_003407433.1; NZ_NVQJ01000071.1.
DR PDB; 3ICO; X-ray; 2.15 A; A/B/C/D=1-247.
DR PDBsum; 3ICO; -.
DR AlphaFoldDB; P9WQP5; -.
DR SMR; P9WQP5; -.
DR STRING; 83332.Rv1445c; -.
DR PaxDb; P9WQP5; -.
DR GeneID; 886617; -.
DR KEGG; mtu:Rv1445c; -.
DR TubercuList; Rv1445c; -.
DR eggNOG; COG0363; Bacteria.
DR OMA; YQLFEFE; -.
DR PhylomeDB; P9WQP5; -.
DR UniPathway; UPA00115; UER00409.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
DR CDD; cd01400; 6PGL; 1.
DR InterPro; IPR005900; 6-phosphogluconolactonase_DevB.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR039104; PGLS.
DR PANTHER; PTHR11054; PTHR11054; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR01198; pgl; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..247
FT /note="6-phosphogluconolactonase"
FT /id="PRO_0000090101"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3ICO"
FT HELIX 11..33
FT /evidence="ECO:0007829|PDB:3ICO"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3ICO"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:3ICO"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:3ICO"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3ICO"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:3ICO"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:3ICO"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:3ICO"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3ICO"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:3ICO"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:3ICO"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:3ICO"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:3ICO"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:3ICO"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:3ICO"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:3ICO"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:3ICO"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:3ICO"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3ICO"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:3ICO"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:3ICO"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:3ICO"
FT STRAND 230..238
FT /evidence="ECO:0007829|PDB:3ICO"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:3ICO"
SQ SEQUENCE 247 AA; 25804 MW; 1639B68A595D7D2C CRC64;
MSSSIEIFPD SDILVAAAGK RLVGAIGAAV AARGQALIVL TGGGNGIALL RYLSAQAQQI
EWSKVHLFWG DERYVPEDDD ERNLKQARRA LLNHVDIPSN QVHPMAASDG DFGGDLDAAA
LAYEQVLAAS AAPGDPAPNF DVHLLGMGPE GHINSLFPHS PAVLESTRMV VAVDDSPKPP
PRRITLTLPA IQRSREVWLL VSGPGKADAV AAAIGGADPV SVPAAGAVGR QNTLWLLDRD
AAAKLPS
