ID A0A1F7CKU3_9BACT Unreviewed; 407 AA.
AC A0A1F7CKU3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Glucose-6-phosphate dehydrogenase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=A3H22_02160 {ECO:0000313|EMBL:OGJ70469.1};
OS Candidatus Peribacteria bacterium RIFCSPLOWO2_12_FULL_55_15.
OC Bacteria; Candidatus Peregrinibacteria; Candidatus Peribacteria.
OX NCBI_TaxID=1801931 {ECO:0000313|EMBL:OGJ70469.1, ECO:0000313|Proteomes:UP000182940};
RN [1] {ECO:0000313|EMBL:OGJ70469.1, ECO:0000313|Proteomes:UP000182940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000256|ARBA:ARBA00004937}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009975}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGJ70469.1}.
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DR EMBL; MFYG01000020; OGJ70469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7CKU3; -.
DR STRING; 1801931.A3H22_02160; -.
DR UniPathway; UPA00115; -.
DR Proteomes; UP000182940; Unassembled WGS sequence.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001282; G6P_DH.
DR InterPro; IPR019796; G6P_DH_AS.
DR InterPro; IPR022675; G6P_DH_C.
DR InterPro; IPR022674; G6P_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022526};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 5..127
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 130..405
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGJ70469.1"
SQ SEQUENCE 407 AA; 45781 MW; B4FF9ABEF0931948 CRC64;
KDMCEVNETM LENFLAHVHY HRGEYATEAD FAAIAKKLAT LEHGWKDVVR LAYLSVPPAV
FAPVLHGLCA GKVHSHSRGG DFRCIVEKPV GQDIESFESI ERALTACFEK NEIFLIDHYL
GKEAVRNIYY LRFANPILER LLKNTLIHHV EITALEDGGT EGRTGYFDHV GTFRDMFQSH
LLEIVSLLTM RMREEEDAFQ DSRQSALEQF YIPPATNLSD VILQGQYDGY ATEDGVAPLS
RTNTFIALKL MSRASRWEGI PFYLRTGKRC GRKVTRITVQ FQETQHVNGG APNRLDIILQ
GEAGMRLYLQ TKLGGTEPAF RPLVLEDPLV CVGDCLPEHG LLLLEAIHGK QQWFLGFEEI
RAAWRLVDPL QAYLEQPSTA LPIYPAGNAG PPAAAAWIAQ DSVQWFP
//
