ID B1XXC2_LEPCP Unreviewed; 297 AA.
AC B1XXC2;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=6-phosphogluconate dehydrogenase NAD-binding {ECO:0000313|EMBL:ACB33903.1};
GN OrderedLocusNames=Lcho_1636 {ECO:0000313|EMBL:ACB33903.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB33903.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB33903.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the HIBADH-related family.
CC {ECO:0000256|ARBA:ARBA00009080}.
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DR EMBL; CP001013; ACB33903.1; -; Genomic_DNA.
DR RefSeq; WP_012346664.1; NC_010524.1.
DR AlphaFoldDB; B1XXC2; -.
DR STRING; 395495.Lcho_1636; -.
DR KEGG; lch:Lcho_1636; -.
DR eggNOG; COG2084; Bacteria.
DR HOGENOM; CLU_035117_1_0_4; -.
DR OrthoDB; 9777604at2; -.
DR Proteomes; UP000001693; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
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; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR029154; HIBADH-like_NADP-bd.
DR InterPro; IPR015815; HIBADH-related.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43060:SF15; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000001693}.
FT DOMAIN 13..171
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 176..294
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 182
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 297 AA; 30843 MW; CDDE0785564969DE CRC64;
MSSKIYEPVA PQRVAFLGLG VMGGPMAGHL ARAGHQVTVY NRTAAKAQAW AAEHGGTFAT
TPREAALGAE IVFACVGNDD DLRSVVLGAD GAFAGMQPGA VFVDHTTASA EVARELAGAA
RVIGLRFIDA PVSGGQAGAV NGALTVMCGG DALAFEAIKP VAMAFSKAVT LLGDSGAGQL
AKMVNQICIA GLVQGLAEAI AFGQNAGLDM NQVLDVIGKG AAQSWQLDNR GKTMVEGRFD
FGFAVDWMRK DLGLVLAEAR RNGSRLPVTA LVDQFYADVQ QHGGQRWDTS SLITRLK
//