CHLB_PROMA
ID CHLB_PROMA Reviewed; 530 AA.
AC Q7VD38;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Pro_0545;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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; AE017126; AAP99590.1; -; Genomic_DNA.
DR RefSeq; NP_874938.1; NC_005042.1.
DR RefSeq; WP_011124699.1; NC_005042.1.
DR PDB; 2YNM; X-ray; 2.10 A; D=1-530.
DR PDBsum; 2YNM; -.
DR AlphaFoldDB; Q7VD38; -.
DR SMR; Q7VD38; -.
DR IntAct; Q7VD38; 2.
DR STRING; 167539.Pro_0545; -.
DR EnsemblBacteria; AAP99590; AAP99590; Pro_0545.
DR GeneID; 54199912; -.
DR KEGG; pma:Pro_0545; -.
DR PATRIC; fig|167539.5.peg.560; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025470_0_0_3; -.
DR OMA; TTFQARD; -.
DR OrthoDB; 363662at2; -.
DR UniPathway; UPA00670; -.
DR Proteomes; UP000001420; 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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Iron;
KW Iron-sulfur; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW Photosynthesis; Reference proteome.
FT CHAIN 1..530
FT /note="Light-independent protochlorophyllide reductase
FT subunit B"
FT /id="PRO_1000048411"
FT REGION 448..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 290
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 425..426
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 69..84
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:2YNM"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2YNM"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 181..194
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 226..240
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 252..266
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 305..317
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 334..343
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 354..364
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 373..382
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 407..419
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 425..433
FT /evidence="ECO:0007829|PDB:2YNM"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 483..490
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 497..510
FT /evidence="ECO:0007829|PDB:2YNM"
FT HELIX 518..527
FT /evidence="ECO:0007829|PDB:2YNM"
SQ SEQUENCE 530 AA; 58729 MW; 7D5A10C8B8D0FF2E CRC64;
MELTLWTYEG PPHIGAMRIA TSMKGLHYVL HAPQGDTYAD LLFTMIERRG SRPPVTYTTF
QARDLGGDTA ELVKGHIFEA VERFKPEALL VGESCTAELI QDQPGSLAKG MGLNIPIVSL
ELPAYSKKEN WGASETFYQL IRGLLKEISE DSSNNAKQSW QEEGRRPRVN LLGPSLLGFR
CRDDVLEIQK ILGENGIDIN VIAPLGASPS DLMRLPKADA NVCLYPEIAE STCLWLERNF
KTPFTKVVPI GVKATQDFLE ELYELLGMEV SNSISNSDQS KLPWYSKSVD SNYLTGKRVF
IFGDGTHVLA AARIANEELG FEVVGIGTYS REMARKVRAA ATELGLEALI TNDYLEVEES
IKECAPELVL GTQMERHSAK RLGIPCAVIS TPMHVQDVPA RYSPQMGWEG ANVIFDDWVH
PLMMGLEEHL IGMFRHDFEF TDGHQSHLGH LGGHASETKT SSKGINQSPN NHSPAGESIH
WTSEGESELA KIPFFVRGKV RRNTEKYARQ AGCREIDGET LLDAKAHFGA
