ID A0A2V5K5K4_9BACL Unreviewed; 436 AA.
AC A0A2V5K5K4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Tartronate semialdehyde reductase {ECO:0000313|EMBL:PYI52973.1};
GN ORFNames=DLM86_18410 {ECO:0000313|EMBL:PYI52973.1};
OS Paenibacillus flagellatus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2211139 {ECO:0000313|EMBL:PYI52973.1, ECO:0000313|Proteomes:UP000247476};
RN [1] {ECO:0000313|EMBL:PYI52973.1, ECO:0000313|Proteomes:UP000247476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DXL2 {ECO:0000313|EMBL:PYI52973.1,
RC ECO:0000313|Proteomes:UP000247476};
RA Dai X.;
RT "Paenibacillus flagellatus sp. nov., isolated from selenium mineral soil.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the HIBADH-related family.
CC {ECO:0000256|ARBA:ARBA00009080}.
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:PYI52973.1}.
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DR EMBL; QJVJ01000008; PYI52973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5K5K4; -.
DR OrthoDB; 9786703at2; -.
DR Proteomes; UP000247476; Unassembled WGS sequence.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
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 Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009875; PilZ_domain.
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 Pfam; PF07238; PilZ; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF141371; PilZ domain-like; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000247476}.
FT DOMAIN 3..162
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 165..284
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 315..420
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
SQ SEQUENCE 436 AA; 47826 MW; 051CCA36C6BDC86E CRC64;
MKKIGFIGLG TMGLPMAANL LRKGYPLTVY NRTADKNAEL LRLGAEAAAT PAEAARDADV
LITMLSNDTA IRQTFYDPNG IMEGIRPGLT VIDCSTISPH TSKTLHAELA EHAVDFLDAP
VTGSKPAAES GTLLFMVGGS EEALQEHRDV FEAMGSRIVY MGASGSGSYA KLAHNTMVGI
NAIGFVEGMA LAAKANVDLE KFYEIVQAGG AASKQAELKG PKILNRDFAT QFSMQLMHKD
LRLASQLTDQ LQLTAPLLNL AKNIYEMGLS KGLGELDLSA IVQCYEEWMD KTVETCKREE
AQPDALLTKQ DLNIERRRSV RVPMNIRLLL SVYQWEQEGA FSGQNIEGTL YDLSDSGLQL
TSHFPLAQDM FVVIHFPQEA GLPPITARII RVFSDGGLFR YGCMLSGLPP YTRIKLEEYI
QLKLQLQEEA ETNEQT
//
