ID A6TTS9_ALKMQ Unreviewed; 298 AA.
AC A6TTS9;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000313|EMBL:ABR49597.1};
GN OrderedLocusNames=Amet_3469 {ECO:0000313|EMBL:ABR49597.1};
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR49597.1, ECO:0000313|Proteomes:UP000001572};
RN [1] {ECO:0000313|Proteomes:UP000001572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419}.
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DR EMBL; CP000724; ABR49597.1; -; Genomic_DNA.
DR RefSeq; WP_012064560.1; NC_009633.1.
DR AlphaFoldDB; A6TTS9; -.
DR STRING; 293826.Amet_3469; -.
DR KEGG; amt:Amet_3469; -.
DR eggNOG; COG1023; Bacteria.
DR HOGENOM; CLU_024540_0_0_9; -.
DR OrthoDB; 9804542at2; -.
DR Proteomes; UP000001572; Chromosome.
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:UP000001572}.
FT DOMAIN 167..294
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
SQ SEQUENCE 298 AA; 32896 MW; 76B28736131BA861 CRC64;
MEIGLIGLGK MGYNLALNMR DHGHRVVAYN RTPDKTQMIE KEGIKGVYSL EALYDSLEGK
RILWMMIPSG EAVDNMIDEL LTFLRSGDIL IDGGNSFYQD TLRRYEKLKD IGIDYIDVGT
SGGIEGARTG ACMMVGGEPH VVEQISSLFQ DISIENGYSF MGTPGSGHYV KMVHNAIEYG
MMQAIGEGFE LLNAGPFSLD FENVAKVWSH GSIIEGLLMR CVLSSFEKSE KLEEIQGIVD
ASGEGQWAVE EALRLKVSMP VISNALFARY KSTDSTKFSE KVVAAMRKEF GGHAIHQK
//
