ID A0A2G4I944_9BACT Unreviewed; 411 AA.
AC A0A2G4I944;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Glucose-6-phosphate dehydrogenase {ECO:0000313|EMBL:PHX94904.1};
DE Flags: Fragment;
GN Name=zwf {ECO:0000313|EMBL:PHX94904.1};
GN ORFNames=CK546_05245 {ECO:0000313|EMBL:PHX94904.1};
OS Pedosphaera sp.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX NCBI_TaxID=2024890 {ECO:0000313|EMBL:PHX94904.1, ECO:0000313|Proteomes:UP000223988};
RN [1] {ECO:0000313|EMBL:PHX94904.1, ECO:0000313|Proteomes:UP000223988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baikal-G1 {ECO:0000313|EMBL:PHX94904.1};
RX PubMed=29079621;
RA Cabello-Yeves P.J., Zemskaya T.I., Rosselli R., Coutinho F.H.,
RA Zakharenko A.S., Blinov V.V., Rodriguez-Valera F.;
RT "Genomes of novel microbial lineages assembled from the sub-ice waters of
RT Lake Baikal.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
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:PHX94904.1}.
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DR EMBL; NSHY01000125; PHX94904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G4I944; -.
DR UniPathway; UPA00115; -.
DR Proteomes; UP000223988; 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 HAMAP; MF_00966; G6PD; 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 NCBIfam; TIGR00871; zwf; 1.
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 28..213
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 215..411
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
FT NON_TER 411
FT /evidence="ECO:0000313|EMBL:PHX94904.1"
SQ SEQUENCE 411 AA; 46312 MW; 8BDE0CC4BE0EA07D CRC64;
MDDLNQLDEL MACRLDDGRK AVTPCTIVIF GASGDLTIRK LIPALYHLFA EKALPNPVRI
VGFARREKDD AAWRGELKAG VEQFSRTKKV DEAVWAEFAA NVSYCQGDLT DAAAYARLGE
KLASFGVPQL RNNLLFYLAI SPSQFAAVVE QLCHANLLKR DETPGEWQRV VVEKPFGTDL
ASALKLNNEL TRFVHEKQIF RIDHYLGKET VQNILMFRFS NAIFEQLWNR TSVDHVQITV
SEKVGVGGRG GYYEESGAMR DMVQNHLLQV LSLIAMEPPV SLDAEAVRDE KVKLLKSIRP
VRDVSTQVVR GQYFAGMVDG KLRNGYRQEE KVKTDSNVET YLALKLFIDN WRWSGVPFFL
RTGKSLPHSA SEVRIQFRPT PNVLFAAKCG LKLDPNAITL RLQPNEGITL R
//
