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CHLB_PROMM
ID   CHLB_PROMM              Reviewed;         536 AA.
AC   Q7V6E8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=chlB {ECO:0000255|HAMAP-Rule:MF_00353}; OrderedLocusNames=PMT_1216;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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 (ChlN-ChlB) 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; chlorophyll
CC       biosynthesis (light-independent). {ECO:0000255|HAMAP-Rule:MF_00353}.
CC   -!- SUBUNIT: Protochlorophyllide reductase is composed of three subunits;
CC       ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN
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; BX548175; CAE21391.1; -; Genomic_DNA.
DR   RefSeq; WP_011130586.1; NC_005071.1.
DR   AlphaFoldDB; Q7V6E8; -.
DR   SMR; Q7V6E8; -.
DR   STRING; 74547.PMT_1216; -.
DR   EnsemblBacteria; CAE21391; CAE21391; PMT_1216.
DR   KEGG; pmt:PMT_1216; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_025470_0_0_3; -.
DR   OMA; TTFQARD; -.
DR   OrthoDB; 363662at2; -.
DR   UniPathway; UPA00670; -.
DR   Proteomes; UP000001423; 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:0036068; P:light-independent chlorophyll 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; Chlorophyll biosynthesis; Iron; Iron-sulfur;
KW   Metal-binding; Nucleotide-binding; Oxidoreductase; Photosynthesis;
KW   Reference proteome.
FT   CHAIN           1..536
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit B"
FT                   /id="PRO_1000048412"
FT   REGION          448..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        292
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         427..428
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
SQ   SEQUENCE   536 AA;  59164 MW;  7D9F389BA48B9EB2 CRC64;
     MELTLWTYEG PPHVGAMRIA SSMEGVHYVL HAPQGDTYAD LLFTMIERRG RRPPVTYTTF
     QARDLGGDTA ELVKGHLHEA VERFNPEALL VGESCTAELI QDQPGSLASG MGFNMPVVGI
     ELPAYSKKEN WGASETFYQL VRGILSKQPS EQSGVSHSPA AWKSQGRRPR VNLLGPTLLG
     FRCRDDILEL EKLLNQHGID VHVVAPLEAR PADLMRLPNA DLNVCLYPEI AEATCLWLER
     NYGMPFSKTV PIGVGATKDF LEELHQLLEM PAPNPGEGAE QSRLPWYSQS VDSNYLTGKR
     VFIFGDGTHA LAAARIADQE LGFKVVGLGT YSREMARPVR AAAKELGLEA LISDDYLAVE
     AAMAEAAPEL VLGTQMERHS AKRLGIPCAV ISTPMHVQDV PARYSPQMGW EGANVIFDSW
     VHPLMMGLEE HLIGMFRHDF EFVDGHQSHL GHLGGHQSQT EQQQSQAATN PSTQSNADSS
     SEESPLWTPE GEAELAKIPF FVRGKVRRNT EKYARQAGCR CIDSETVYDA KVHFRA
 
 
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