ID A0A1C4A2L6_9ENTR Unreviewed; 331 AA.
AC A0A1C4A2L6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=6-phosphogluconolactonase {ECO:0000256|HAMAP-Rule:MF_01605};
DE Short=6-P-gluconolactonase {ECO:0000256|HAMAP-Rule:MF_01605};
DE EC=3.1.1.31 {ECO:0000256|HAMAP-Rule:MF_01605};
GN Name=pgl {ECO:0000256|HAMAP-Rule:MF_01605};
GN ORFNames=GA0061070_1003113 {ECO:0000313|EMBL:SCB88878.1};
OS Kosakonia oryziphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Kosakonia.
OX NCBI_TaxID=1005667 {ECO:0000313|EMBL:SCB88878.1, ECO:0000313|Proteomes:UP000198515};
RN [1] {ECO:0000313|Proteomes:UP000198515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=REICA_142 {ECO:0000313|Proteomes:UP000198515};
RA Varghese N., Submissions Spin;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-
CC phosphogluconate. {ECO:0000256|HAMAP-Rule:MF_01605}.
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 Evidence={ECO:0000256|HAMAP-Rule:MF_01605};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 2/3. {ECO:0000256|HAMAP-Rule:MF_01605}.
CC -!- SIMILARITY: Belongs to the cycloisomerase 2 family.
CC {ECO:0000256|ARBA:ARBA00005564, ECO:0000256|HAMAP-Rule:MF_01605}.
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DR EMBL; FMBC01000003; SCB88878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4A2L6; -.
DR OrthoDB; 9790815at2; -.
DR UniPathway; UPA00115; UER00409.
DR Proteomes; UP000198515; Unassembled WGS sequence.
DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_01605; 6P_gluconolactonase; 1.
DR InterPro; IPR022528; 6-phosphogluconolactonase_YbhE.
DR InterPro; IPR019405; Lactonase_7-beta_prop.
DR InterPro; IPR011045; N2O_reductase_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR30344:SF9; 6-PHOSPHOGLUCONOLACTONASE; 1.
DR PANTHER; PTHR30344; 6-PHOSPHOGLUCONOLACTONASE-RELATED; 1.
DR Pfam; PF10282; Lactonase; 1.
DR SUPFAM; SSF50974; Nitrous oxide reductase, N-terminal domain; 1.
DR SUPFAM; SSF50960; TolB, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01605};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526, ECO:0000256|HAMAP-
KW Rule:MF_01605};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01605}.
SQ SEQUENCE 331 AA; 36291 MW; FFE4DDFC50324E0C CRC64;
MKQTVYTASP ESQQIHVWRL NSEGTLTLVQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV
IAYRIAPDDG ALTFEAEAPL PGSPTHISTD RSGRFLFSAS YNAGSVSVTR LEDGIPTQNV
DVVEGLDGCH SANISPDNRT LWVPALKQDR ICLFTLADDG NLTAQNPAEV TTVEGAGPRH
MVFHPNARFG YCVNELNSSV DVWQLSDAHG KIECVQTLDI MPSDFTDTRW AADIHITPDG
RHLYTCDRTA SLLTIFSVSE DGSVLSLEGF QPTETQPRGF NIDKSGKYLI AAGQKSHHIA
LYKISGEQGL LTEKARYAVG QGPMWVVVNA F
//