ID   Y4VI_SINFN              Reviewed;         548 AA.
AC   Q53217;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=Uncharacterized short-chain type dehydrogenase/reductase y4vI;
DE            EC=1.-.-.-;
GN   OrderedLocusNames=NGR_a01150; ORFNames=y4vI;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8796346; DOI=10.1101/gr.6.7.590;
RA   Freiberg C., Perret X., Broughton W.J., Rosenthal A.;
RT   "Sequencing the 500-kb GC-rich symbiotic replicon of Rhizobium sp. NGR234
RT   using dye terminators and a thermostable 'sequenase': a beginning.";
RL   Genome Res. 6:590-600(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- DOMAIN: Contains two SDR domains.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA92424.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z68203; CAA92424.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00090; AAB91897.1; -; Genomic_DNA.
DR   RefSeq; NP_444110.1; NC_000914.2.
DR   RefSeq; WP_010875153.1; NC_000914.2.
DR   AlphaFoldDB; Q53217; -.
DR   SMR; Q53217; -.
DR   KEGG; rhi:NGR_a01150; -.
DR   PATRIC; fig|394.7.peg.100; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_040287_0_0_5; -.
DR   OrthoDB; 9805986at2; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   CDD; cd05233; SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR24321; DEHYDROGENASES, SHORT CHAIN; 1.
DR   PANTHER; PTHR24321:SF16; SHORT-CHAIN DEHYDROGENASE REDUCTASE SDR; 1.
DR   Pfam; PF13561; adh_short_C2; 2.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Multifunctional enzyme; Oxidoreductase; Plasmid; Reference proteome;
KW   Repeat.
FT   CHAIN           1..548
FT                   /note="Uncharacterized short-chain type
FT                   dehydrogenase/reductase y4vI"
FT                   /id="PRO_0000054889"
FT   REGION          1..250
FT                   /note="Short-chain dehydrogenase/reductase 1"
FT   REGION          271..548
FT                   /note="Short-chain dehydrogenase/reductase 2"
FT   ACT_SITE        154
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   ACT_SITE        420
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         12..37
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         280..304
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   548 AA;  57594 MW;  399598C5DF17C23F CRC64;
     MDDRQVQPGR VIVVTGAAGG IGRALVDIFA ANGDVVVAVD LPDSGVIELG QNLGEPHLGL
     EVDVSREDDV VALRALLEKR FSRIEVLVNN AGIGPTMAAT ADTALEDFQR ALAINLVGAY
     SVACETAKLM KPGAAIVNVA SLAGLLGNPK RSAYAASKAG LISITKSLAC RWASRGIRVT
     AVAPGHVRTP MVAELERAGK LDVSAIRRRV PLGRIARPDE IARAVRFLAS AQASYITGST
     LVVDGGWMSV NQPGGAHQAQ DRTPGAEFMR PVEDTDARTV IVMGGATGVG AAIARRFAEN
     GDTVVIADGD GEEAVKLAGL LGDKHLSRRV DRTVETEVVS LFEELRERFG HLDVFVNGMN
     EILVPNTEES PEVLKRILDV NLTGAFTCVR EAAISMRSGS VILNLGASLS LSPLAPSHAY
     GAYNAGIDML TRCTAAELGP LGIRTATVAP GYIRTCAANR LAAVAGMDSA SLRQRIPLGR
     VGDAEEVAEA AYFLASFDAS YINGSILHVD GGLISSREAG WGSEVDGAIS AEMRPQRRPA
     ARWRLLSP
//