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Database: UniProt
Entry: A8ANV1_CITK8
LinkDB: A8ANV1_CITK8
Original site: A8ANV1_CITK8 
ID   A8ANV1_CITK8            Unreviewed;       197 AA.
AC   A8ANV1;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Probable UbiX-like flavin prenyltransferase {ECO:0000256|HAMAP-Rule:MF_01986};
DE            EC=2.5.1.129 {ECO:0000256|HAMAP-Rule:MF_01986};
DE   AltName: Full=Phenolic acid decarboxylase subunit B {ECO:0000256|HAMAP-Rule:MF_01986};
DE            Short=PAD {ECO:0000256|HAMAP-Rule:MF_01986};
GN   OrderedLocusNames=CKO_04098 {ECO:0000313|EMBL:ABV15164.1};
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV15164.1, ECO:0000313|Proteomes:UP000008148};
RN   [1] {ECO:0000313|EMBL:ABV15164.1, ECO:0000313|Proteomes:UP000008148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696
RC   {ECO:0000313|Proteomes:UP000008148};
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the non-oxidative decarboxylation and
CC       detoxification of phenolic derivatives. Flavin prenyltransferase that
CC       catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for
CC       phenolic acid decarboxylase. {ECO:0000256|HAMAP-Rule:MF_01986}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2;
CC         Xref=Rhea:RHEA:37743, ChEBI:CHEBI:43474, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:87467, ChEBI:CHEBI:88052; EC=2.5.1.129;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01986};
CC   -!- SUBUNIT: Homododecamer. {ECO:0000256|HAMAP-Rule:MF_01986}.
CC   -!- SIMILARITY: Belongs to the UbiX/PAD1 family. YclB subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01986}.
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DR   EMBL; CP000822; ABV15164.1; -; Genomic_DNA.
DR   RefSeq; WP_012134854.1; NC_009792.1.
DR   AlphaFoldDB; A8ANV1; -.
DR   STRING; 290338.CKO_04098; -.
DR   GeneID; 45137737; -.
DR   KEGG; cko:CKO_04098; -.
DR   HOGENOM; CLU_074522_0_1_6; -.
DR   OrthoDB; 9781577at2; -.
DR   Proteomes; UP000008148; Chromosome.
DR   GO; GO:0106141; F:flavin prenyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1950; Flavin prenyltransferase-like; 1.
DR   HAMAP; MF_01984; ubiX_pad; 1.
DR   HAMAP; MF_01986; ubiX_pad_yclB; 1.
DR   InterPro; IPR036551; Flavin_trans-like.
DR   InterPro; IPR003382; Flavoprotein.
DR   InterPro; IPR004507; UbiX-like.
DR   InterPro; IPR032901; UbiX_pad_YclB.
DR   NCBIfam; TIGR00421; ubiX_pad; 1.
DR   NCBIfam; NF041206; VdcB; 1.
DR   PANTHER; PTHR43374; FLAVIN PRENYLTRANSFERASE; 1.
DR   PANTHER; PTHR43374:SF1; FLAVIN PRENYLTRANSFERASE PAD1, MITOCHONDRIAL; 1.
DR   Pfam; PF02441; Flavoprotein; 1.
DR   SUPFAM; SSF52507; Homo-oligomeric flavin-containing Cys decarboxylases, HFCD; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism {ECO:0000256|HAMAP-Rule:MF_01986};
KW   Detoxification {ECO:0000256|HAMAP-Rule:MF_01986};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_01986};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01986};
KW   Prenyltransferase {ECO:0000256|ARBA:ARBA00022602, ECO:0000256|HAMAP-
KW   Rule:MF_01986}; Reference proteome {ECO:0000313|Proteomes:UP000008148};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01986}.
FT   DOMAIN          1..173
FT                   /note="Flavoprotein"
FT                   /evidence="ECO:0000259|Pfam:PF02441"
FT   BINDING         9..11
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01986"
FT   BINDING         36
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01986"
FT   BINDING         87..90
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01986"
FT   BINDING         122
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01986"
SQ   SEQUENCE   197 AA;  21578 MW;  258D41043478F28F CRC64;
     MRLIVGMTGA TGAPLGIALL QALRQMPTVE THLVMSKWAK TTIELETPYS ARDVAGLADY
     CHNPADQAAT ISSGSFRTDG MIIMPCSMKT LAGIRAGYAE GLVGRAADVV LKEGRKLVLV
     PREMPLSTIH LENMLALSRM GVAMVPPMPA FYNHPQTIDD ITQHIVARVL DQFGLEHPRA
     RRWQGLQQAQ NFSQENE
//
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