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Database: UniProt
Entry: B4D7K2_9BACT
LinkDB: B4D7K2_9BACT
Original site: B4D7K2_9BACT 
ID   B4D7K2_9BACT            Unreviewed;       575 AA.
AC   B4D7K2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Precorrin-3B synthase {ECO:0000313|EMBL:EDY17619.1};
DE            EC=1.7.7.1 {ECO:0000313|EMBL:EDY17619.1};
GN   ORFNames=CfE428DRAFT_4917 {ECO:0000313|EMBL:EDY17619.1};
OS   Chthoniobacter flavus Ellin428.
OC   Bacteria; Verrucomicrobiota; Spartobacteria; Chthoniobacterales;
OC   Chthoniobacteraceae; Chthoniobacter.
OX   NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY17619.1, ECO:0000313|Proteomes:UP000005824};
RN   [1] {ECO:0000313|EMBL:EDY17619.1, ECO:0000313|Proteomes:UP000005824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin428 {ECO:0000313|EMBL:EDY17619.1,
RC   ECO:0000313|Proteomes:UP000005824};
RX   PubMed=21460085; DOI=10.1128/JB.00295-11;
RA   Kant R., van Passel M.W., Palva A., Lucas S., Lapidus A.,
RA   Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S.,
RA   Larimer F.W., Land M.L., Hauser L., Sangwan P., de Vos W.M., Janssen P.H.,
RA   Smidt H.;
RT   "Genome sequence of Chthoniobacter flavus Ellin428, an aerobic
RT   heterotrophic soil bacterium.";
RL   J. Bacteriol. 193:2902-2903(2011).
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:EDY17619.1}.
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DR   EMBL; ABVL01000018; EDY17619.1; -; Genomic_DNA.
DR   RefSeq; WP_006982238.1; NZ_ABVL01000018.1.
DR   AlphaFoldDB; B4D7K2; -.
DR   STRING; 497964.CfE428DRAFT_4917; -.
DR   GeneID; 78183166; -.
DR   eggNOG; COG0155; Bacteria.
DR   InParanoid; B4D7K2; -.
DR   Proteomes; UP000005824; Unassembled WGS sequence.
DR   GO; GO:0048307; F:ferredoxin-nitrite reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR   Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 1.
DR   InterPro; IPR012798; Cbl_synth_CobG-like.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   NCBIfam; TIGR02435; CobG; 1.
DR   PANTHER; PTHR32439; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR32439:SF0; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01077; NIR_SIR; 2.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EDY17619.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005824}.
FT   DOMAIN          104..166
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          176..326
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
FT   DOMAIN          354..420
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          434..555
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   575 AA;  64072 MW;  5F848F5BEC4E9180 CRC64;
     MSTASLPISN INGQPLNEEQ MRYLTGFFAG VAARGQRFSD VEAPPILAKS IAHEDLVFEE
     RVKKELHPLD AYPLLLEHAA SNKAPEKEEV FRFKWNGLFY LSPNKEAFMA RLRIPGGQLR
     TFQLRELANI AKQLTTGYVQ ITTRANLQMR LIQPKDTPEF LHRIQSVGLH ARGSGADNIR
     NLTANPTAGV DPHELIDVMP LCHEMGQIIL NDRSFYDLPR KFNIAYDGGG LIGTVEDTND
     VGCKAVKMGE EIFFRIALGG ATGHKAFARD LGVLVKPEEL NKVVSAIVRV YIEHGNRGDR
     KKARLKHLLE KWTLEQYLEE TEKLLGYQLQ RVPLDPALIE YPGQKLPHSH VGVYPQKQKG
     LNYVGVAMPV GQITPKQMIR IAEIADLYGS GEIRLTVWQN FVIPNVPDHF VATVKKALRK
     IGFDTQQSNL RSGIIACTGN SYCKFAQANT KGHAMELADY LDKRIKLDQP VNIHLTGCPH
     SCAQHYMGDI GLLGTKAKIA GESVDGYHIF VGGGFGASQA VGRQVFNAID FESAKPLVEK
     MLRGYLRHRE GNETFQAFTA RHDLNALQGI FSNEE
//
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