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BCHB_RHORT
ID   BCHB_RHORT              Reviewed;         546 AA.
AC   Q2RWR9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Light-independent protochlorophyllide reductase subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE            Short=DPOR subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE            Short=LI-POR subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE            EC=1.3.7.7 {ECO:0000255|HAMAP-Rule:MF_00353};
GN   Name=bchB {ECO:0000255|HAMAP-Rule:MF_00353}; OrderedLocusNames=Rru_A0622;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
CC   -!- FUNCTION: Component of the dark-operative protochlorophyllide reductase
CC       (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of
CC       protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This
CC       reaction is light-independent. The NB-protein (BchN-BchB) is the
CC       catalytic component of the complex. {ECO:0000255|HAMAP-Rule:MF_00353}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2
CC         phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-
CC         4S]-[ferredoxin]; Xref=Rhea:RHEA:28202, Rhea:RHEA-COMP:10002,
CC         Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33722, ChEBI:CHEBI:33723, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83348, ChEBI:CHEBI:83350, ChEBI:CHEBI:456216; EC=1.3.7.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00353};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00353};
CC       Note=Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at
CC       the heterodimer interface by residues from both subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00353};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC       biosynthesis (light-independent). {ECO:0000255|HAMAP-Rule:MF_00353}.
CC   -!- SUBUNIT: Protochlorophyllide reductase is composed of three subunits;
CC       BchL, BchN and BchB. Forms a heterotetramer of two BchB and two BchN
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00353}.
CC   -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. {ECO:0000255|HAMAP-
CC       Rule:MF_00353}.
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DR   EMBL; CP000230; ABC21426.1; -; Genomic_DNA.
DR   RefSeq; WP_011388380.1; NC_007643.1.
DR   RefSeq; YP_425713.1; NC_007643.1.
DR   AlphaFoldDB; Q2RWR9; -.
DR   SMR; Q2RWR9; -.
DR   STRING; 269796.Rru_A0622; -.
DR   PRIDE; Q2RWR9; -.
DR   EnsemblBacteria; ABC21426; ABC21426; Rru_A0622.
DR   KEGG; rru:Rru_A0622; -.
DR   PATRIC; fig|269796.9.peg.677; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_025470_0_0_5; -.
DR   OMA; TTFQARD; -.
DR   OrthoDB; 363662at2; -.
DR   PhylomeDB; Q2RWR9; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000001929; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
DR   GO; GO:0016636; F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
DR   Gene3D; 1.10.8.550; -; 1.
DR   HAMAP; MF_00353; ChlB_BchB; 1.
DR   InterPro; IPR013580; LI-POR_suB-like_C.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR042298; P-CP_red_C.
DR   InterPro; IPR005969; Protochl_reductB.
DR   InterPro; IPR016209; Protochlorophyllide_Rdtase.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   Pfam; PF08369; PCP_red; 1.
DR   PIRSF; PIRSF000163; PCP_ChlB; 1.
DR   TIGRFAMs; TIGR01278; DPOR_BchB; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; Bacteriochlorophyll biosynthesis;
KW   Chlorophyll biosynthesis; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotide-binding; Oxidoreductase; Photosynthesis; Reference proteome.
FT   CHAIN           1..546
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit B"
FT                   /id="PRO_0000324043"
FT   REGION          443..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        287
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
FT   BINDING         36
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
FT   BINDING         422..423
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
SQ   SEQUENCE   546 AA;  58351 MW;  13D6165846036461 CRC64;
     MRLTVWTYEG PPQVGAMRVA TAMRGVHYVV HAPQGDSYAD LLFTMIERRP GRPAVSYTSF
     QARDLGTDTA ALFKTAAADA VARFQPEALL VGSSCTGELI QDDPGGLAKA LGLSIPVIPL
     ELPSYQRKEN WGAAETFYRL VRTMAGPAAP APGTPRAPRP AGQRPRCNLL GPTALGFRHR
     DDVQAVVALL GRMGVDVAVV APLGASPADL ARLGEADFNV VLYPEIADTA VRWLERAFGQ
     PSVRTVPIGV GATRAFIAEV AAVAGVDPAP ALAEESLRLP WWSRSVDSTY LTGKRVFIFG
     DATHAVAAAR VATEEFGFEV VGLGTYAREY ARELRACAGA LGLEALITDD YLDVEAAIAD
     AHPDLVLGTQ MERHIAKRLG VPCAVISAPV HVQDFPARTA PQMGFDGANV LFDTWVHPLM
     MGLEEHLLMM FRDDFEFHGD AAPSHLSAHR PTGEAVGDAV GEPPAAPRDQ AAPAATLDGS
     AAQSDPARTT PPGAPSWEDS AEKELRKVPF FVRGKARRNT ERFAAERGLA SISVETLYDA
     KAHFGR
 
 
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