ID A0A0D1KZ24_9MYCO Unreviewed; 335 AA.
AC A0A0D1KZ24;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Glucose-6-phosphate dehydrogenase {ECO:0000313|EMBL:KIU14045.1};
DE Flags: Fragment;
GN ORFNames=TL10_26405 {ECO:0000313|EMBL:KIU14045.1};
OS Mycolicibacterium llatzerense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=280871 {ECO:0000313|EMBL:KIU14045.1, ECO:0000313|Proteomes:UP000032221};
RN [1] {ECO:0000313|EMBL:KIU14045.1, ECO:0000313|Proteomes:UP000032221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLUC14 {ECO:0000313|EMBL:KIU14045.1,
RC ECO:0000313|Proteomes:UP000032221};
RA Greninger A.L., Langelier C., Cunningham G., Chiu C.Y., Miller S.;
RT "Genome sequence of Mycobacterium llatzerense and Mycobacterium immunogenum
RT recovered from brain abscess.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KIU14045.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JXST01000054; KIU14045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1KZ24; -.
DR STRING; 280871.TL10_26405; -.
DR OrthoDB; 9802739at2; -.
DR UniPathway; UPA00115; -.
DR Proteomes; UP000032221; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000032221}.
FT DOMAIN 34..217
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 219..334
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
FT NON_TER 335
FT /evidence="ECO:0000313|EMBL:KIU14045.1"
SQ SEQUENCE 335 AA; 36952 MW; 3AB37F6EAA8BDDD3 CRC64;
MSSSSSAAPA DWGNPLRDKL DKRLPRIPGP CAVVIFGVTG DLATKKLMPA IYDLANRGLL
PPTFALVGFA RRDWQDEDFG DIVLKAVQAH ARTPFRQEVW DRLNEGIRFV QGTFDDADSF
ARLKETLDKL DAERGTGGNH AFYLSIPPKA FPTVCEQLST SGLARPEDDR WSRVVIEKPF
GHDLESARSL NKVVNSVFPE SSVFRIDHYL GKETVQNILA LRFANQLFDP IWNAHHVDHV
QITMAEDIGL GGRGGYYDGV GAARDVIQNH LTQLLALTAM EEPVSFSPAE LQAEKIKVLS
ATRLAEPVDQ NTSRGQYTAG WQGGEKVVGL LEEEG
//