ID A0A0G2J518_9SYNE Unreviewed; 555 AA.
AC A0A0G2J518;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Light-independent protochlorophyllide reductase subunit B {ECO:0000256|HAMAP-Rule:MF_00353};
DE Short=DPOR subunit B {ECO:0000256|HAMAP-Rule:MF_00353};
DE Short=LI-POR subunit B {ECO:0000256|HAMAP-Rule:MF_00353};
DE EC=1.3.7.7 {ECO:0000256|HAMAP-Rule:MF_00353};
GN Name=chlB {ECO:0000256|HAMAP-Rule:MF_00353};
GN ORFNames=TE42_04410 {ECO:0000313|EMBL:KKZ12512.1};
OS Candidatus Synechococcus spongiarum SP3.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1604020 {ECO:0000313|EMBL:KKZ12512.1, ECO:0000313|Proteomes:UP000035067};
RN [1] {ECO:0000313|EMBL:KKZ12512.1, ECO:0000313|Proteomes:UP000035067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP3 {ECO:0000313|EMBL:KKZ12512.1};
RA Burgsdorf I., Slaby B.M., Handley K.M., Haber M., Blom J., Marshall C.W.,
RA Gilbert J.A., Hentschel U., Steindler L.;
RT "Lifestyle Evolution in Cyanobacterial Symbionts of Sponges.";
RL Submitted (JAN-2015) 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:0000256|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:0000256|HAMAP-Rule:MF_00353};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00353};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004800}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis (light-independent). {ECO:0000256|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:0000256|HAMAP-Rule:MF_00353}.
CC -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. {ECO:0000256|HAMAP-
CC Rule:MF_00353}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKZ12512.1}.
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DR EMBL; JXQG01000019; KKZ12512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2J518; -.
DR PATRIC; fig|1604020.3.peg.141; -.
DR UniPathway; UPA00669; -.
DR UniPathway; UPA00670; -.
DR Proteomes; UP000035067; Unassembled WGS sequence.
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:0030494; P:bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
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; 1.20.89.20; -; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
DR Gene3D; 1.10.8.550; Proto-chlorophyllide reductase 57 kD subunit B; 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 NCBIfam; TIGR01278; DPOR_BchB; 1.
DR PANTHER; PTHR33712; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR PANTHER; PTHR33712:SF7; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR Pfam; PF08369; PCP_red; 1.
DR PIRSF; PIRSF000163; PCP_ChlB; 1.
DR SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00353};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00353};
KW Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171, ECO:0000256|HAMAP-
KW Rule:MF_00353};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00353};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00353};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00353};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00353};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00353};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_00353}.
FT DOMAIN 12..439
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
FT DOMAIN 506..550
FT /note="Light-independent protochlorophyllide reductase
FT subunit B-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08369"
FT REGION 463..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 307
FT /note="Proton donor"
FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_00353"
FT BINDING 442..443
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00353"
SQ SEQUENCE 555 AA; 60405 MW; BA4DFFC75B810C07 CRC64;
MELTLWTYEG PPHVGAMRIA TSMEGVHYVL HAPQGDTYAD LLFTMIERRG KRPPVTYTTF
QARDLGGDTA EMVKVSVRDA VERFQPQALL VGESCTAELI QDQPGALAGG MGLPIPVVNL
ELPAYSKKEN WGAAETFYQL VRRLLKDRIP PPGTARPGRA PGVRPKVNLL GPSALGFRCR
DDVTEVCRLL GEIGVQVSVV APLGASPADL QRIPEADLNI CLYPEVAKPV CDWLERQFAM
PCVYTVPIGI GATRDFLQEV GAALGVDVTM ALRPDVVGAS DLWSPQLHGG STERARSRLP
WYSRSVDSTY LTGKRVFVFA DGTHALAAAR IATAELGFEL VGLGTYSRES AKLVRAAAKG
YGLEALITDD YLAVEQAISE AAPELVLGTQ MERHIAKRLS IPCAVISTPI HVQDVPARYG
PQMGWEGANV IFDTWVHPLM MGLEEHLIGM FREDFEFVDG HQSHLHVGGS QPVDSPKPKE
PQDPPEPAPA ASVSVSTASA DKARRWSQEG LAELGKVPFF VRGKVRRNTE AFAQTQGIDL
ITVDTLYEAK AHYGR
//
