ID   NODG_RHIME              Reviewed;         245 AA.
AC   P06234;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Nodulation protein G;
DE   AltName: Full=Host-specificity of nodulation protein C;
GN   Name=nodG; Synonyms=hsnC; OrderedLocusNames=RA0467; ORFNames=SMa0854;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymA (megaplasmid 1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RCR2011 / SU47;
RX   PubMed=3020515; DOI=10.1093/nar/14.18.7453;
RA   Debelle F., Sharma S.B.;
RT   "Nucleotide sequence of Rhizobium meliloti RCR2011 genes involved in host
RT   specificity of nodulation.";
RL   Nucleic Acids Res. 14:7453-7472(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=17246400; DOI=10.1093/genetics/117.2.191;
RA   Fisher R.F., Swanson J.A., Mulligan J.T., Long S.R.;
RT   "Extended region of nodulation genes in Rhizobium meliloti 1021. II.
RT   Nucleotide sequence, transcription start sites and protein products.";
RL   Genetics 117:191-201(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481432; DOI=10.1073/pnas.161294798;
RA   Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA   Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA   Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA   Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA   Long S.R.;
RT   "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT   meliloti pSymA megaplasmid.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
CC   -!- FUNCTION: Proposed to modify Nod factor fatty acyl chain.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; X04379; CAA27962.1; -; Genomic_DNA.
DR   EMBL; Y00604; CAA68649.1; -; Genomic_DNA.
DR   EMBL; AE006469; AAK65125.1; -; Genomic_DNA.
DR   PIR; C24706; C24706.
DR   PIR; C95320; C95320.
DR   RefSeq; NP_435713.1; NC_003037.1.
DR   RefSeq; WP_003532825.1; NC_003037.1.
DR   AlphaFoldDB; P06234; -.
DR   SMR; P06234; -.
DR   EnsemblBacteria; AAK65125; AAK65125; SMa0854.
DR   GeneID; 25012153; -.
DR   GeneID; 61599270; -.
DR   KEGG; sme:SMa0854; -.
DR   PATRIC; fig|266834.11.peg.477; -.
DR   HOGENOM; CLU_010194_1_3_5; -.
DR   OMA; KHMVDAG; -.
DR   PRO; PR:P06234; -.
DR   Proteomes; UP000001976; Plasmid pSymA.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR011284; 3oxo_ACP_reduc.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01830; 3oxo_ACP_reduc; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NAD; Nodulation; Oxidoreductase; Plasmid; Reference proteome.
FT   CHAIN           1..245
FT                   /note="Nodulation protein G"
FT                   /id="PRO_0000054733"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         11..35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   245 AA;  26088 MW;  230A5A09E772530E CRC64;
     MFELTGRKAL VTGASGAIGG AIARVLHAQG AIVGLHGTQI EKLETLATEL GDRVKLFPAN
     LANRDEVKAL GQRAEADLEG VDILVNNAGI TKDGLFLHMA DPDWDIVLEV NLTAMFRLTR
     EITQQMIRRR NGRIINVTSV AGAIGNPGQT NYCASKAGMI GFSKSLAQEI ATRNITVNCV
     APGFIESAMT DKLNHKQKEK IMVAIPIHRM GTGTEVASAV AYLASDHAAY VTGQTIHVNG
     GMAMI