ID   MOCR_RHIML              Reviewed;         493 AA.
AC   P49309;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Probable rhizopine catabolism regulatory protein MocR;
GN   Name=mocR;
OS   Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=L5-30;
RX   PubMed=7845353; DOI=10.1007/bf00279746;
RA   Rossbach S., Kulpa D.A., Rossbach U., de Bruijn F.J.;
RT   "Molecular and genetic characterization of the rhizopine catabolism
RT   (mocABRC) genes of Rhizobium meliloti L5-30.";
RL   Mol. Gen. Genet. 245:11-24(1994).
CC   -!- FUNCTION: Could play a regulatory role in the transcription of the moc
CC       genes for rhizopine catabolism. Could also have an aminotransferase
CC       activity.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000305};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the class-I
CC       pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.
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DR   EMBL; X78503; CAA55271.1; -; Genomic_DNA.
DR   PIR; S51574; S51574.
DR   AlphaFoldDB; P49309; -.
DR   SMR; P49309; -.
DR   PATRIC; fig|382.53.peg.1554; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd07377; WHTH_GntR; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF00392; GntR; 1.
DR   SMART; SM00345; HTH_GNTR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS50949; HTH_GNTR; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; DNA-binding; Pyridoxal phosphate; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..493
FT                   /note="Probable rhizopine catabolism regulatory protein
FT                   MocR"
FT                   /id="PRO_0000050654"
FT   DOMAIN          10..78
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT   DNA_BIND        38..57
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT   MOD_RES         319
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   493 AA;  55128 MW;  CE1B0FCD9CC7175C CRC64;
     MLVLDRDADV PMHRQLYEKL RAEILAGHLK ADTRLPPTRM MAEDLGVSRN TVITTYDALL
     AEGYLESRSG SGTWVATLPP DAVTARNSVG RAGAPSLSSR GMRMAAQPRD RTIPDRIAFH
     PGYPEIKAFP FSTWARLLKR HARYSHEDLY GYHWVTGHPR LKAAIAEYLR ASRGVECAPE
     QVIVVNGTQA ALDILARMLV DEGDICWMEE PGYIGAQNSL LSAGAKLVPL PVERDGWSLE
     DETRPSPRLI FVTPSCQWPL GCLMRMEDRL RLLQIGERHD AWIVEDDYDS EYRFRGRPVP
     AMQGLDKSGR VIYMGTFAKT LFPSLRIGFI VVPPQLADGF KRVVSNTGHY PSLLLQAALA
     DFISEGYFAT HLRRMRRLYA ERQKVFVALC RRHLADWLTI DENDAGMQLV ARFTRALEDE
     VLWRAAQGQG VNFSPLSRQF FHSPPQQGAI LGYAGIDPKT MREGINSLRS AFLALESSGA
     LPLDRATAAP RGC