ID B3EM59_CHLPB Unreviewed; 996 AA.
AC B3EM59;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 18-JUN-2025, entry version 96.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ACE03437.1};
GN OrderedLocusNames=Cphamn1_0473 {ECO:0000313|EMBL:ACE03437.1};
OS Chlorobium phaeobacteroides (strain BS1).
OC Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales;
OC Chlorobiaceae; Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=331678 {ECO:0000313|EMBL:ACE03437.1};
RN [1] {ECO:0000313|EMBL:ACE03437.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS1 {ECO:0000313|EMBL:ACE03437.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001101; ACE03437.1; -; Genomic_DNA.
DR AlphaFoldDB; B3EM59; -.
DR STRING; 331678.Cphamn1_0473; -.
DR KEGG; cpb:Cphamn1_0473; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_0_0_10; -.
DR OrthoDB; 596405at2; -.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd00368; Molybdopterin-Binding; 1.
DR FunFam; 3.30.70.20:FF:000035; Iron hydrogenase 1; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR042204; 2Fe-2S-bd_N.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR054351; NADH_UbQ_OxRdtase_ferredoxin.
DR NCBIfam; NF009410; PRK12771.1; 1.
DR PANTHER; PTHR42783; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR42783:SF3; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN-RELATED; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF22117; Fer4_Nqo3; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 3..81
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 616..635
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 655..688
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 696..752
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 996 AA; 107738 MW; E73D326A1F3519D6 CRC64;
MSDTVTVFLN NVSVQAPAGA TIREVAAANG VHIPTFCYDD RLQPYASCFL CVVEVEKARG
LLPACSTVVA EGMVIHTDSE KVITARKTAL ELLLSDHAGD CVAPCEATCP AHIDIQGYIA
HIANGNPEAA VRLIKKSNPL PVVCGRICPH PCELQCRRGL VDEPVSINPL KRFAAEYELE
HGAYLPETAP DTGKRVAVVG GGPAGLSAAY YLRQMGHAVV IFEALPELGG MVRYGIPRFR
LPWELLDNEI QSILDLGVEV RTGKKLGEDF TIASLKKEGF DAVLLAVGAH RAKPMGVSRE
EAPGVIGGID FLRKVVLGEE VALGNQVAVI GGGDTAMDCA RVARRKGAEV TLLYRRTQAE
MPALPMEQDE TMEEGVEFMF LTAPTEVLVD ENGQVSHLRV ISMKLGDPDE SGRRRPVPVE
GSEEDLQFDM VISAIGQDPD MSCVEDDPEK PELTRWNTFV YDEKTNVTSQ KGVFAAGDCA
FGPDTVIRAV GEGQRSAKAI DLYLSGADVH LQNEYAITRG RVQDLKMQDF ASRYTHEKRV
QDSVLPAEER LKDGGWVPIN IGLEKIQAMA EASRCIECGC NARFDCDLRT YATEYGADDA
RFRGDKRKYD NDERHPLIRI EGDKCITCGS CVRICTEVRG IGALCFINRG FSTRIGPNFD
DPLQLTGCDA CGMCIDVCPT GALAPNTGKE AGPWEAVDAM TSCSSCSRGC GLMVATAEGR
VVRVQSIDGD PVNNAVICAE GRFGYQLLDD RGSHDDQSSV EESKAMLASA EELAVVVSPR
LTIEQTYAAA RLARRYNGRL LYISGEEGAS EKPDSVRYAK ISGEANTALL DRLHAGGISI
VEELKADTVV LVGAQIPSCN GQKIIAINPA KGNEECYFVM ADPLQTEGMT LNRDGNLCMV
HAVVPKPEEV PDCHALLAEL AGEDSLKELE SLRNALADEI EELSVIRNPD SDKRLFHSGL
EPVLTAVSPD TRERAFAAHL KAIGMYEPRC ACACGD
//