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Database: UniProt
Entry: D3RP76_ALLVD
LinkDB: D3RP76_ALLVD
Original site: D3RP76_ALLVD 
ID   D3RP76_ALLVD            Unreviewed;       481 AA.
AC   D3RP76;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Chlorophyllide reductase subunit Z {ECO:0000256|ARBA:ARBA00019776};
DE            EC=1.3.7.15 {ECO:0000256|ARBA:ARBA00012326};
DE   AltName: Full=Chlorin reductase subunit Z {ECO:0000256|ARBA:ARBA00032447};
GN   OrderedLocusNames=Alvin_2556 {ECO:0000313|EMBL:ADC63466.1};
OS   Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS   10441 / D) (Chromatium vinosum).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=572477 {ECO:0000313|EMBL:ADC63466.1, ECO:0000313|Proteomes:UP000001441};
RN   [1] {ECO:0000313|EMBL:ADC63466.1, ECO:0000313|Proteomes:UP000001441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D
RC   {ECO:0000313|Proteomes:UP000001441};
RX   PubMed=22675582; DOI=10.4056/sigs.2335270;
RA   Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA   Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT   "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL   Stand. Genomic Sci. 5:311-330(2011).
CC   -!- FUNCTION: Converts chlorophylls (Chl) into bacteriochlorophylls (BChl)
CC       by reducing ring B of the tetrapyrrole.
CC       {ECO:0000256|ARBA:ARBA00003934}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + ADP +
CC         2 oxidized [2Fe-2S]-[ferredoxin] + phosphate = 3-devinyl-3-(1-
CC         hydroxyethyl)chlorophyllide a + ATP + H(+) + H2O + 2 reduced [2Fe-
CC         2S]-[ferredoxin]; Xref=Rhea:RHEA:48948, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:90791, ChEBI:CHEBI:90792,
CC         ChEBI:CHEBI:456216; EC=1.3.7.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00001586};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-deacetyl-3-vinylbacteriochlorophyllide a + ADP + 2 oxidized
CC         [2Fe-2S]-[ferredoxin] + phosphate = ATP + chlorophyllide a + H(+) +
CC         H2O + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:37051,
CC         Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:43474, ChEBI:CHEBI:83348,
CC         ChEBI:CHEBI:83373, ChEBI:CHEBI:456216; EC=1.3.7.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00000965};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP + bacteriochlorophyllide a + 2 oxidized [2Fe-2S]-
CC         [ferredoxin] + phosphate = 3-acetyl-3-devinylchlorophyllide a + ATP +
CC         H(+) + H2O + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:48944,
CC         Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:43474, ChEBI:CHEBI:90794,
CC         ChEBI:CHEBI:90795, ChEBI:CHEBI:456216; EC=1.3.7.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00000410};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004800}.
CC   -!- SUBUNIT: Chlorophyllide reductase is composed of three subunits; BchX,
CC       BchY and BchZ. Forms a heterodimer of one BchY and one BchZ subunit.
CC       {ECO:0000256|ARBA:ARBA00011283}.
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DR   EMBL; CP001896; ADC63466.1; -; Genomic_DNA.
DR   RefSeq; WP_012971735.1; NC_013851.1.
DR   AlphaFoldDB; D3RP76; -.
DR   STRING; 572477.Alvin_2556; -.
DR   KEGG; alv:Alvin_2556; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_564837_0_0_6; -.
DR   OrthoDB; 5713965at2; -.
DR   UniPathway; UPA00669; -.
DR   Proteomes; UP000001441; Chromosome.
DR   GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
DR   GO; GO:0030494; P:bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR   InterPro; IPR010244; BchZ.
DR   InterPro; IPR013580; LI-POR_suB-like_C.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR016209; Protochlorophyllide_Rdtase.
DR   NCBIfam; TIGR02014; BchZ; 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   4: Predicted;
KW   Bacteriochlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023181};
KW   Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001441}.
FT   DOMAIN          12..395
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
FT   DOMAIN          425..475
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit B-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08369"
SQ   SEQUENCE   481 AA;  53090 MW;  60463A38A7FDC009 CRC64;
     MLINDLDRAG GYWGSVYVFT AIKGLQVIID GPVGCENLPV TAVLHYTDGL PPHELPVVVT
     GLGEEELGQS GTEQAMRRAF ETLDPKQPSV VVTGSIAEMI GGGVTPEGTG IVRFLPRTID
     EDQWQSANRA MYWLWTQYGQ KKGAAKSKPK PRAAGDKPRV NIIGPVYGTF NMPSDLAEIR
     RLVEGIGAEV NLSFPLGSHL DDVPRLADAD ANICLYREFG RTLCEALDKP YLQAPIGLHS
     TTKFLRALGE ILGLDPEPFI EREKHTTIKP IWDLWRSVTQ DFFGTASFGV SASETYSRGL
     RHFLEDELGL PCNFAFARRP GVKIDNDAIR AAVHEKPPLI LFGSYNERMY LTEKGARATY
     IPASFPGTVI RRHTGTPFMG YAGATYLVQE VCNALFDALF HIIPLGTELD KVEATPARMH
     RELPWDEDAR ARFDAIVESQ PVLVRISAAK RLRDAAERAA RTAGEERVTV ERVEATQSTL
     I
//
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