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STCD_RHIME
ID   STCD_RHIME              Reviewed;         678 AA.
AC   O87278;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Probable N-methylproline demethylase;
DE            EC=1.-.-.-;
DE   AltName: Full=Stachydrine utilization protein StcD;
GN   Name=stcD; Synonyms=stcD2; OrderedLocusNames=RB1010; ORFNames=SMb21570;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymB (megaplasmid 2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=1021;
RX   PubMed=9758825; DOI=10.1128/aem.64.10.3954-3960.1998;
RA   Phillips D.A., Sande E.S., Vriezen J.A.C., de Bruijn F.J., Le Rudulier D.,
RA   Joseph C.M.;
RT   "A new genetic locus in Sinorhizobium meliloti is involved in stachydrine
RT   utilization.";
RL   Appl. Environ. Microbiol. 64:3954-3960(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481431; DOI=10.1073/pnas.161294698;
RA   Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA   Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT   "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT   endosymbiont Sinorhizobium meliloti.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN   [3]
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: Possible NADH-dependent oxidase, functions as a demethylase
CC       that converts N-methylproline to proline. {ECO:0000269|PubMed:9758825}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P42593};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P42593};
CC   -!- PATHWAY: Amine and polyamine degradation; stachydrine degradation.
CC   -!- INDUCTION: By stachydrine.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC63907.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF016307; AAC63907.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL591985; CAC49410.1; -; Genomic_DNA.
DR   PIR; B95968; B95968.
DR   RefSeq; NP_437550.1; NC_003078.1.
DR   RefSeq; WP_010975854.1; NC_003078.1.
DR   AlphaFoldDB; O87278; -.
DR   SMR; O87278; -.
DR   STRING; 266834.SM_b21570; -.
DR   EnsemblBacteria; CAC49410; CAC49410; SM_b21570.
DR   GeneID; 61600970; -.
DR   KEGG; sme:SM_b21570; -.
DR   PATRIC; fig|266834.11.peg.5935; -.
DR   eggNOG; COG0446; Bacteria.
DR   eggNOG; COG1902; Bacteria.
DR   HOGENOM; CLU_012153_1_2_5; -.
DR   OMA; NQACIAY; -.
DR   BioCyc; MetaCyc:MON-2221; -.
DR   UniPathway; UPA00255; -.
DR   Proteomes; UP000001976; Plasmid pSymB.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019504; P:stachydrine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
DR   Pfam; PF00724; Oxidored_FMN; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; FMN; NAD; Oxidoreductase; Plasmid; Reference proteome.
FT   CHAIN           1..678
FT                   /note="Probable N-methylproline demethylase"
FT                   /id="PRO_0000194491"
FT   BINDING         59
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         102
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         220
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         299
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         321..322
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         396
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         415
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         423
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         433
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         460
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   CONFLICT        6..7
FT                   /note="LL -> FF (in Ref. 1; AAC63907)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63..91
FT                   /note="VSKDSPPVFNNLLAYRDEIVPWIREMTDA -> SRRTARRSSTICSPTGTRS
FT                   CRGSGRCRP (in Ref. 1; AAC63907)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95..97
FT                   /note="EGA -> RGR (in Ref. 1; AAC63907)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        591
FT                   /note="Y -> I (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   678 AA;  74684 MW;  329E22EDD928ED1B CRC64;
     MPNDPLLQPY QLKHLTLRNR IIVTAHEPAY PEDGMPKERY RAYTVERARG GVAMTMTAGS
     AAVSKDSPPV FNNLLAYRDE IVPWIREMTD AVHEEGAVIM IQLTHLGRRT RWDKGDWLPV
     VAPSHHREAA HRAFPKKIED WDIDRIIKDF ADAAERMKAG GMDGVELEAY GHLIDQFASP
     LTNELDGPYG GSLDNRMRFC FDVLKAIRAR VGDEFILGVR YTADECLPGG TDKAEGLEIS
     KRLKESGLID YLNIIRGHID TDPGLTDVIP IQGMANSPHL DFAGEIRAAT NFPTFHAAKI
     PDVATARHAI ASGKVDMVGM TRAHMTDPHI VRKIIEKREE DIRPCVGANY CLDRIYQGGA
     AYCIHNAATG RELTMPHSIA KAHCRRKVVV VGTGPAGLEA ARVAGERGHE VIVFEAASDP
     GGQVRLTAQS PRRREMISII DWRMSQCEKL GVTFHFNTWA EAEAIQAESP DVVIIATGGL
     PHTEVLSRGN ELVVSAWDII SGDAKPGTNV LIFDDAGDHA ALQAAEFLAT AGARVEIMTP
     DRSFAPEVMA MNLVPYMRCL QKLDVTFTVT YRLEAVEKSG NELVAHVGSD YGGISKQRTF
     DQVVVNHGTI PLDELYFELK PFSSNLGEIA HDQMIAGEPQ SVVRNAEGKF QLFRIGDAVA
     ARNTHAAIYD ALRLLKDI
 
 
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