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Database: UniProt
Entry: A0A0D1KZ24_9MYCO
LinkDB: A0A0D1KZ24_9MYCO
Original site: A0A0D1KZ24_9MYCO 
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}.
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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
//
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