ID Q73ZB6_MYCPA Unreviewed; 817 AA.
AC Q73ZB6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 107.
DE RecName: Full=Glucose-6-phosphate dehydrogenase (NADP(+)) {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=MAP_1687 {ECO:0000313|EMBL:AAS04004.1};
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS04004.1, ECO:0000313|Proteomes:UP000000580};
RN [1] {ECO:0000313|EMBL:AAS04004.1, ECO:0000313|Proteomes:UP000000580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580};
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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}.
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DR EMBL; AE016958; AAS04004.1; -; Genomic_DNA.
DR AlphaFoldDB; Q73ZB6; -.
DR STRING; 262316.MAP_1687; -.
DR KEGG; mpa:MAP_1687; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_345750_0_0_11; -.
DR UniPathway; UPA00115; -.
DR Proteomes; UP000000580; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000580}.
FT DOMAIN 32..205
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 207..348
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..799
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ SEQUENCE 817 AA; 87948 MW; CAAD0862102F0002 CRC64;
MATQKPQTIS YPAPEARPRR HHTDPLDPHV IVLFGATGDL AKRKLIPGLA YLDQSELAPD
IQIVATSLED LSNDEFRELA KNAIDSFGTH KLTPDQWRNF ADIITYIPQS AGSDALAAAV
AEAEAKLGPN VRRLHYLSVP PKAARAVITM LRDAKLVERS RVVMEKPFGT DLASAVALND
FVHQTFEESQ IFRIDHFLGK EAAQNILAFR FANGLFEPIW NRNFIDHIQI DIPEALGLDQ
RASFYEETGA YKDMVVTHLF QVMAFVVMEP PTALEPFAIS EEKNKVFRSM LPVKPSNVVR
GQYIGYREED GVAKDSDTET FIALKVGIDN WRWAGVPVYL RTGKRMAEGI RHHLDRVQGG
TADHVPARVG GGHAGARPPD VRSCGQFAGV AVVLRQAARP RHETGQAVHA ILHPGDRNRG
GRAGGLRTAH PGRDARRPHP VHHRRRHRIT VGAFRRAAQR PATGQAVPAG DVGPQRNSPV
DRAQRVAAAV RARVARSPDP TPEWAAEKCC GSAQFGAEIT DGLAEFPEDF VVGQLEAVVG
VHPLGGQAGD APAGGLQVVA GRAALAEPDQ FGHVDVQSVL APGAAHRPGA FVGEHPHVGD
VLGGQPAARR AERGDVVQQP VLGVRRQVGQ QPLGDPGGTG AAVKAVVAQR CWPVIAQIDG
DGAALGGRLR AQPGQGVGLE GDDLGLVDLE HHGARRPGQP VGPRVEPGGQ DDGLANAGSG
RGAEEIVEKP RPHRDLLAPL LQRHRHVVGV ERDLAVQHPD EEGMPDRAHQ RFGEPVVEQR
VRTARGQRPG GRDHGRGRPH AGGQIPAVAL GTCRTGR
//
