位置:首页 > 蛋白库 > COFH_CYAP4
COFH_CYAP4
ID   COFH_CYAP4              Reviewed;         381 AA.
AC   B8HP19;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase {ECO:0000255|HAMAP-Rule:MF_01612};
DE            EC=2.5.1.147 {ECO:0000255|HAMAP-Rule:MF_01612};
DE   AltName: Full=FO synthase subunit 2 {ECO:0000255|HAMAP-Rule:MF_01612};
GN   Name=cofH {ECO:0000255|HAMAP-Rule:MF_01612};
GN   OrderedLocusNames=Cyan7425_3281;
OS   Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Cyanothecaceae; Cyanothece; unclassified Cyanothece.
OX   NCBI_TaxID=395961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7425 / ATCC 29141;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
CC   -!- FUNCTION: Catalyzes the radical-mediated synthesis of 5-amino-5-(4-
CC       hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-
CC       ribitylamino)uracil and L-tyrosine. {ECO:0000255|HAMAP-Rule:MF_01612}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-
CC         methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-
CC         hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-
CC         methionine; Xref=Rhea:RHEA:55200, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15934, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58315, ChEBI:CHEBI:59789, ChEBI:CHEBI:77846,
CC         ChEBI:CHEBI:85936; EC=2.5.1.147; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01612};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01612};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000255|HAMAP-Rule:MF_01612};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01612}.
CC   -!- SUBUNIT: Consists of two subunits, CofG and CofH. {ECO:0000255|HAMAP-
CC       Rule:MF_01612}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. CofH family.
CC       {ECO:0000255|HAMAP-Rule:MF_01612}.
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; CP001344; ACL45606.1; -; Genomic_DNA.
DR   RefSeq; WP_012628669.1; NC_011884.1.
DR   AlphaFoldDB; B8HP19; -.
DR   SMR; B8HP19; -.
DR   STRING; 395961.Cyan7425_3281; -.
DR   EnsemblBacteria; ACL45606; ACL45606; Cyan7425_3281.
DR   KEGG; cyn:Cyan7425_3281; -.
DR   eggNOG; COG1060; Bacteria.
DR   HOGENOM; CLU_040406_1_0_3; -.
DR   OMA; ATMMFGS; -.
DR   OrthoDB; 419725at2; -.
DR   UniPathway; UPA00072; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0044689; F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01612; FO_synth_sub2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR045567; CofH/MnqC-like_C.
DR   InterPro; IPR019940; CofH_family.
DR   InterPro; IPR034405; F420.
DR   InterPro; IPR020050; FO_synthase_su2.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR43076; PTHR43076; 1.
DR   Pfam; PF19288; CofH_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDF00293; ((2_3_4_5-tetrahydroxypentyl)a; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   TIGRFAMs; TIGR03551; F420_cofH; 1.
DR   TIGRFAMs; TIGR00423; TIGR00423; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..381
FT                   /note="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-
FT                   hydroxyphenyl transferase"
FT                   /id="PRO_1000215706"
FT   DOMAIN          59..306
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         73
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01612"
FT   BINDING         77
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01612"
FT   BINDING         80
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01612"
SQ   SEQUENCE   381 AA;  42352 MW;  D7A5B5A315B1A640 CRC64;
     MAVPTLSETL TTLLHRVLQG EDLTPEEGVF LLQQWDPEAL TVIRQTSDRL RQQQVGDTVT
     YVVNRNINFT NICEQHCSFC AFRRDEDQPG AYWLGFDEIL AKTGEAVERG ATEICMQGGL
     HPGAKLQGHS LAYYLKLVET IKTTFPTLHL HAFSPQEVQF IAREDGLSYA QVITALRDAG
     VNSMPGTAAE VLVDEVRRVI CPEKINTATW LEIISTAHAL GVPTTSTMLS GQIETPQQQI
     EHLFLLRSLQ QKAIQQDYPA RFTEFILLPY VGQSAPKPLR KRVGRDQPVL QDALLLTAVA
     RIFLGNWIVN HQPSWVKLGL AGATEALIWG CNDLGGTLME EHITSMAGAQ GGTCRSVENL
     QQAIASLNRP YRERTTLYGY L
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024