CHLB_SYNE7
ID CHLB_SYNE7 Reviewed; 508 AA.
AC Q8GJN0; Q31M51;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 95.
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};
GN OrderedLocusNames=Synpcc7942_1838; ORFNames=sem0009;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Holtman C.K., Sandoval P., Chen Y., Socias T., McMurtry S., Gonzalez A.,
RA Salinas I., Golden S.S., Youderian P.;
RT "Synechococcus elongatus PCC7942 cosmid 4G8.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; AY157498; AAN46159.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57868.1; -; Genomic_DNA.
DR RefSeq; WP_011244566.1; NC_007604.1.
DR AlphaFoldDB; Q8GJN0; -.
DR SMR; Q8GJN0; -.
DR STRING; 1140.Synpcc7942_1838; -.
DR PRIDE; Q8GJN0; -.
DR EnsemblBacteria; ABB57868; ABB57868; Synpcc7942_1838.
DR KEGG; syf:Synpcc7942_1838; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025470_0_0_3; -.
DR OMA; TTFQARD; -.
DR OrthoDB; 363662at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1838-MON; -.
DR UniPathway; UPA00670; -.
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.
FT CHAIN 1..508
FT /note="Light-independent protochlorophyllide reductase
FT subunit B"
FT /id="PRO_0000219806"
FT ACT_SITE 294
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 429..430
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
FT CONFLICT 246
FT /note="P -> A (in Ref. 1; AAN46159)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="A -> G (in Ref. 1; AAN46159)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="D -> K (in Ref. 1; AAN46159)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="R -> C (in Ref. 1; AAN46159)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="A -> T (in Ref. 1; AAN46159)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="S -> N (in Ref. 1; AAN46159)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="A -> T (in Ref. 1; AAN46159)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 56643 MW; 8C3F41A779099668 CRC64;
MKLAYWMYAG PAHIGTLRIS SSFRNVHAIM HAPLGDDYFN VMRSMLERER NFTPVTTSVV
DRNVLARGSQ EKVIDNILRK DTEERPDLIV LTPTCTSSIL QEDLQNFVER AKESAQCDVL
LADVNHYRVN ELQAADRTLE QIVRFYLDRA QRQGTLPSQR TEQPSVNILG MTTLGFHNRH
DTTELQRLMA DLGITVNAVI PAGASVEELQ HLPRAWFNLV PYREVGLLTA QYLQDTFDQP
MVAIAPMGIT ATADCIRQIQ QVLNQQGAAV DFEPFIDRQT RFASEAAWFS HSIDCQNLTG
KRAVVFGDNT HAAAFTKILS REMGIHVVLA GTYCKHDADW FEAEVAGYCD RVLISDDHNA
IADAIAELEP AAIFGTQMER HVGKRLNIPC GVIAAPVHIQ NFPVGYRPFV GYEGANQIVD
LVYNSFTLGM EDHLLEIFGG HDTKEVLTKT VSAGSDLDWK PDGLTELNRI PGFVRGKVKR
NTEKYAREQG LTAITAEVLY AAKEALGA
