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Database: UniProt
Entry: G4E5B2_9GAMM
LinkDB: G4E5B2_9GAMM
Original site: G4E5B2_9GAMM 
ID   G4E5B2_9GAMM            Unreviewed;       314 AA.
AC   G4E5B2;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Chlorophyllide reductase iron protein subunit X {ECO:0000313|EMBL:EGZ46238.1};
DE            EC=1.18.6.1 {ECO:0000313|EMBL:EGZ46238.1};
GN   ORFNames=ThisiDRAFT_1491 {ECO:0000313|EMBL:EGZ46238.1};
OS   Thiorhodospira sibirica ATCC 700588.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thiorhodospira.
OX   NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ46238.1};
RN   [1] {ECO:0000313|EMBL:EGZ46238.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ46238.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J.,
RA   Frigaard N.-U., Bryant D., Woyke T.;
RT   "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC       {ECO:0000256|ARBA:ARBA00005504, ECO:0000256|RuleBase:RU003688}.
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:EGZ46238.1}.
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DR   EMBL; AGFD01000026; EGZ46238.1; -; Genomic_DNA.
DR   RefSeq; WP_006787504.1; NZ_MU255056.1.
DR   AlphaFoldDB; G4E5B2; -.
DR   STRING; 765914.ThisiDRAFT_1491; -.
DR   PATRIC; fig|765914.3.peg.1487; -.
DR   eggNOG; COG1348; Bacteria.
DR   OrthoDB; 9815116at2; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0018697; F:carbonyl sulfide nitrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016163; F:nitrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0030494; P:bacteriochlorophyll biosynthetic process; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR010246; BchX.
DR   InterPro; IPR030655; NifH/chlL_CS.
DR   InterPro; IPR000392; NifH/frxC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR02016; BchX; 1.
DR   PANTHER; PTHR42864; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1.
DR   PANTHER; PTHR42864:SF2; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1.
DR   Pfam; PF00142; Fer4_NifH; 1.
DR   PRINTS; PR00091; NITROGNASEII.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00746; NIFH_FRXC_1; 1.
DR   PROSITE; PS00692; NIFH_FRXC_2; 1.
DR   PROSITE; PS51026; NIFH_FRXC_3; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU003688};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003688};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003688};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU003688};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003688};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003688};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003688,
KW   ECO:0000313|EMBL:EGZ46238.1}.
SQ   SEQUENCE   314 AA;  33125 MW;  8420844B73602E79 CRC64;
     MTLSSQDAQA ASAKETQIIA IYGKGGIGKS FTLANLSYTL AQQGKKVLLI GCDPKSDTTS
     LLFGGRACPT IIETSARKKL AGEEVTISDV CFKRDGVFAM ELGGPEVGRG CGGRGIIHGF
     ELLEKLGFNE WGFDYVLLDF LGDVVCGGFG LPISRDMCQK VIVVGSNDLQ SLYVVNNVCS
     AVEYFRKLGG NVGVAGMVIN KDDGTGEAQT FAAQVGIPVL ATIPANEEIR RKSASYQIVS
     GADSAWAPLF NQLAENVTTA PPMHPTALSQ DALLGLFAGD AVGRDVVLEP ATLEDMCGQT
     VTKKPSLEVI YDDA
//
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