(data stored in SCRATCH zone)

SWISSPROT: B2UHV9_RALPJ

ID   B2UHV9_RALPJ            Unreviewed;       346 AA.
AC   B2UHV9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=FAD:protein FMN transferase {ECO:0000256|PIRNR:PIRNR006268, ECO:0000256|RuleBase:RU363002};
DE            EC=2.7.1.180 {ECO:0000256|PIRNR:PIRNR006268, ECO:0000256|RuleBase:RU363002};
DE   AltName: Full=Flavin transferase {ECO:0000256|PIRNR:PIRNR006268};
GN   OrderedLocusNames=Rpic_4057 {ECO:0000313|EMBL:ACD29160.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29160.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Flavin transferase that catalyzes the transfer of the
CC       FMN moiety of FAD and its covalent binding to the hydroxyl group
CC       of a threonine residue in a target flavoprotein.
CC       {ECO:0000256|RuleBase:RU363002}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-
CC         [protein] + H(+); Xref=Rhea:RHEA:36847, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11061, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:74257, ChEBI:CHEBI:456215;
CC         EC=2.7.1.180; Evidence={ECO:0000256|PIRNR:PIRNR006268,
CC         ECO:0000256|RuleBase:RU363002};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006268-2};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006268-2};
CC       Note=Magnesium. Can also use manganese.
CC       {ECO:0000256|PIRSR:PIRSR006268-2};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|RuleBase:RU363002}.
CC   -!- SIMILARITY: Belongs to the ApbE family.
CC       {ECO:0000256|PIRNR:PIRNR006268, ECO:0000256|RuleBase:RU363002}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001069; ACD29160.1; -; Genomic_DNA.
DR   RefSeq; WP_012430153.1; NC_010678.1.
DR   STRING; 402626.Rpic_4057; -.
DR   EnsemblBacteria; ACD29160; ACD29160; Rpic_4057.
DR   GeneID; 6285393; -.
DR   KEGG; rpi:Rpic_4057; -.
DR   PATRIC; fig|402626.5.peg.301; -.
DR   eggNOG; ENOG4105CJ2; Bacteria.
DR   eggNOG; COG1477; LUCA.
DR   HOGENOM; HOG000080809; -.
DR   KO; K03734; -.
DR   OMA; WRVGIQH; -.
DR   OrthoDB; 2021063at2; -.
DR   BioCyc; RPIC402626:GH94-4056-MONOMER; -.
DR   Proteomes; UP000002566; Chromosome 2.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0017013; P:protein flavinylation; IEA:UniProtKB-UniRule.
DR   InterPro; IPR024932; ApbE.
DR   InterPro; IPR003374; ApbE-like_sf.
DR   PANTHER; PTHR30040; PTHR30040; 1.
DR   Pfam; PF02424; ApbE; 1.
DR   PIRSF; PIRSF006268; ApbE; 1.
DR   SUPFAM; SSF143631; SSF143631; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2UHV9.
DR   SWISS-2DPAGE; B2UHV9.
KW   Cell inner membrane {ECO:0000256|RuleBase:RU363002};
KW   Cell membrane {ECO:0000256|RuleBase:RU363002};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   FAD {ECO:0000256|PIRNR:PIRNR006268, ECO:0000256|PIRSR:PIRSR006268-1,
KW   ECO:0000256|RuleBase:RU363002};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR006268,
KW   ECO:0000256|RuleBase:RU363002};
KW   Lipoprotein {ECO:0000256|RuleBase:RU363002,
KW   ECO:0000313|EMBL:ACD29160.1};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR006268,
KW   ECO:0000256|PIRSR:PIRSR006268-2, ECO:0000256|RuleBase:RU363002};
KW   Membrane {ECO:0000256|RuleBase:RU363002};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR006268,
KW   ECO:0000256|PIRSR:PIRSR006268-2, ECO:0000256|RuleBase:RU363002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566};
KW   Signal {ECO:0000256|RuleBase:RU363002};
KW   Transferase {ECO:0000256|PIRNR:PIRNR006268,
KW   ECO:0000256|RuleBase:RU363002}.
FT   SIGNAL        1     32       {ECO:0000256|RuleBase:RU363002}.
FT   CHAIN        33    346       FAD:protein FMN transferase.
FT                                {ECO:0000256|RuleBase:RU363002}.
FT                                /FTId=PRO_5005967861.
FT   NP_BIND     122    124       FAD. {ECO:0000256|PIRSR:PIRSR006268-1}.
FT   NP_BIND     179    181       FAD. {ECO:0000256|PIRSR:PIRSR006268-1}.
FT   METAL       182    182       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR006268-2}.
FT   BINDING     185    185       FAD. {ECO:0000256|PIRSR:PIRSR006268-1}.
FT   BINDING     266    266       FAD. {ECO:0000256|PIRSR:PIRSR006268-1}.
FT   BINDING     268    268       FAD. {ECO:0000256|PIRSR:PIRSR006268-1}.
SQ   SEQUENCE   346 AA;  37262 MW;  FF6CED48EE3B6230 CRC64;
     MHPLPPSNLG RRRCLAGVPL LAVGMFVRPA LADPTVERAS TQLLGTQIDI IAQDARPGAA
     GAAMRAAFVE MARLECLMSR YRPDSQVSAL ARAAGRNPVP VAPEVMSVFK LARQVSEQSR
     GAFDITVGAY SGWNFDPEHS RIPSSSELAR ERRFVNYRDV VLDERHGSVY LRRPGMRLDL
     GGIAKLPILE AGMRVLRQHG IRDAMINGGG DVVASGKLQG HEWRVGLRDP LAPERLLGVV
     TLSDGVVASS GDYERYFMHN GQRFHHVLDP ETGLPAHGPH GVTLVSRDVD DVNGLGAAIM
     AAGTATGQRM LAPMLARVDA LIVGSGVRPW MSAGMATRLR QFSASS
//

If you have problems or comments...

PBIL Back to PBIL home page