ID   NODG_AZOBR              Reviewed;         246 AA.
AC   P17611;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Nodulation protein G;
GN   Name=nodG;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=1538694; DOI=10.1007/bf00292706;
RA   Vieille C., Elmerich C.;
RT   "Characterization of an Azospirillum brasilense Sp7 gene homologous to
RT   Alcaligenes eutrophus phbB and to Rhizobium meliloti nodG.";
RL   Mol. Gen. Genet. 231:375-384(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=2243795; DOI=10.1093/nar/18.21.6435;
RA   Delledonne M., Porcari R., Fogher C.;
RT   "Nucleotide sequence of the nodG gene of Azospirillum brasilense.";
RL   Nucleic Acids Res. 18:6435-6435(1990).
CC   -!- FUNCTION: Proposed to modify Nod factor fatty acyl chain.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA37101.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X64772; CAA46021.1; -; Genomic_DNA.
DR   EMBL; X52913; CAA37101.1; ALT_FRAME; Genomic_DNA.
DR   PIR; S20485; DEKCNG.
DR   RefSeq; WP_035669664.1; NZ_WFKD01000096.1.
DR   AlphaFoldDB; P17611; -.
DR   SMR; P17611; -.
DR   GeneID; 56450830; -.
DR   OrthoDB; 1601931at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0018454; F:acetoacetyl-CoA reductase activity; IEA:InterPro.
DR   GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:InterPro.
DR   InterPro; IPR011283; Acetoacetyl-CoA_reductase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01829; AcAcCoA_reduct; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NAD; Nodulation; Oxidoreductase.
FT   CHAIN           1..246
FT                   /note="Nodulation protein G"
FT                   /id="PRO_0000054732"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         8..32
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        101..108
FT                   /note="DKAQWDAV -> TRPSGMRF (in Ref. 2; CAA37101)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   246 AA;  25718 MW;  A3419C7E4D4750C0 CRC64;
     MSQKIALVTG AMGGLGTAIC QALAKDGCIV AANCLPNFEP AAAWLGQQEA LGFKFYVAEG
     DVSDFESCKA MVAKIEADLG PVDILVNNAG ITRDKFFAKM DKAQWDAVIA TNLSSLFNVT
     QQVSPKMAER GWGRIINISS VNGVKGQAGQ TNYSAAKAGV IGFTKALAAE LATKGVTVNA
     IAPGYIGTDM VMAIREDIRQ AITDSVPMKR LGRPDEIGGA VSYLASEIAG YVTGSTLNIN
     GGLNYQ