ID A0A1E8CPL3_9MICO Unreviewed; 388 AA.
AC A0A1E8CPL3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=6-phosphogluconate dehydrogenase (Decarboxylating) {ECO:0000313|EMBL:OFE14205.1};
GN ORFNames=BA895_11320 {ECO:0000313|EMBL:OFE14205.1};
OS Humibacillus sp. DSM 29435.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Humibacillus.
OX NCBI_TaxID=1869167 {ECO:0000313|EMBL:OFE14205.1, ECO:0000313|Proteomes:UP000175826};
RN [1] {ECO:0000313|Proteomes:UP000175826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29435 {ECO:0000313|Proteomes:UP000175826};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419}.
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:OFE14205.1}.
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DR EMBL; MAST01000054; OFE14205.1; -; Genomic_DNA.
DR RefSeq; WP_070194104.1; NZ_MAST01000054.1.
DR AlphaFoldDB; A0A1E8CPL3; -.
DR STRING; 1869167.BA895_11320; -.
DR OrthoDB; 9804542at2; -.
DR Proteomes; UP000175826; Unassembled WGS sequence.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:InterPro.
DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR004849; 6DGDH_YqeC.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006114; 6PGDH_C.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006183; Pgluconate_DH.
DR NCBIfam; TIGR00872; gnd_rel; 1.
DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11811:SF67; 6-PHOSPHOGLUCONATE DEHYDROGENASE YQEC-RELATED; 1.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PRINTS; PR00076; 6PGDHDRGNASE.
DR SMART; SM01350; 6PGD; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064};
KW Reference proteome {ECO:0000313|Proteomes:UP000175826}.
FT DOMAIN 162..361
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT REGION 297..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 388 AA; 41247 MW; B1FD1040C1B609A0 CRC64;
MQLGLIGLGK MGGNMRERLR RAGHEVVGYD RNPDVADVRT MAAMVKKLEA PRVVWVMVPS
GDPTRETIAK LAELLEPGDL VIDGGNSRFT DDFENAKMLA AQKIGYVDCG VSGGIWGLDN
GYGLMCGGDK KWVTKAMPIF DALRPEGPRD EGFVHAGKVG AGHYTKMVHN GIEYGLMAAY
AEGFELLEKK DIVTDVPGAF KAWSRGTVVR SWLLDLMVDA LEANPHLDDV SDYTNDSGEG
RWTVEEAIAM SVPMPVISAS LFARFASRQQ SSPTMQAVAA LRGGFGGHQV MTIAEGDKLR
EGAVPTRSTK KESAPTQAKK RASAKKASSQ SAAVASQANV GAARKAATSK KAPATQATDM
ADTARGQARA AKAAPARKSV GKRAAKKA
//
