ID D3RTQ1_ALLVD Unreviewed; 338 AA.
AC D3RTQ1;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000313|EMBL:ADC62560.1};
GN OrderedLocusNames=Alvin_1628 {ECO:0000313|EMBL:ADC62560.1};
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477 {ECO:0000313|EMBL:ADC62560.1, ECO:0000313|Proteomes:UP000001441};
RN [1] {ECO:0000313|EMBL:ADC62560.1, ECO:0000313|Proteomes:UP000001441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D
RC {ECO:0000313|Proteomes:UP000001441};
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC {ECO:0000256|ARBA:ARBA00004959}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419}.
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DR EMBL; CP001896; ADC62560.1; -; Genomic_DNA.
DR RefSeq; WP_012970834.1; NC_013851.1.
DR AlphaFoldDB; D3RTQ1; -.
DR STRING; 572477.Alvin_1628; -.
DR KEGG; alv:Alvin_1628; -.
DR eggNOG; COG1023; Bacteria.
DR HOGENOM; CLU_024540_0_0_6; -.
DR OrthoDB; 9804542at2; -.
DR UniPathway; UPA00115; -.
DR Proteomes; UP000001441; 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:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
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.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 3: Inferred from homology;
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001441}.
FT DOMAIN 184..318
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
SQ SEQUENCE 338 AA; 36431 MW; 37C14EFD94FCE3A5 CRC64;
MHIGMIGLGR MGANMVRRLL RAGHQCVVYN RNPAKAQALV DEGAIAISDP AEFRARMESP
RHIWLMVPAA AVGGVIEDLI PHLEPGDALI DGGNSHYHDD LVHAERLRPL GLHLVDCGTS
GGVWGLERGY CLMIGGEPDV VERLDPIFAA LAPGAGEIPR TAGRSGPPSR AEQGYLHCGP
NGAGHFVKMV HNGIEYALMG AYAEGFNLLR HAGIGREDRA SDAETAPLAH PEHYQYDIPL
AEVAEVWRRG SVIASWLLDL TANALHEDPR LDAFGGRVSD SGEGRWTALA AIETGTPAPL
LTTALYERFG SRGEGDFANQ LLSAMRYQFG GHHEKPKD
//