ID A0A0A6PDV5_9GAMM Unreviewed; 594 AA.
AC A0A0A6PDV5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KHD08925.1};
GN ORFNames=PN36_18370 {ECO:0000313|EMBL:KHD08925.1};
OS Candidatus Thiomargarita nelsonii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thiomargarita.
OX NCBI_TaxID=1003181 {ECO:0000313|EMBL:KHD08925.1, ECO:0000313|Proteomes:UP000030428};
RN [1] {ECO:0000313|EMBL:KHD08925.1, ECO:0000313|Proteomes:UP000030428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hydrate Ridge {ECO:0000313|EMBL:KHD08925.1};
RX PubMed=27199933; DOI=10.3389/fmicb.2016.00603;
RA Flood B.E., Fliss P., Jones D.S., Dick G.J., Jain S., Kaster A.K.,
RA Winkel M., Mussmann M., Bailey J.;
RT "Single-Cell (Meta-)Genomics of a Dimorphic Candidatus Thiomargarita
RT nelsonii Reveals Genomic Plasticity.";
RL Front. Microbiol. 7:603-603(2016).
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:KHD08925.1}.
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DR EMBL; JSZA02000072; KHD08925.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A6PDV5; -.
DR Proteomes; UP000030428; Unassembled WGS sequence.
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:InterPro.
DR Gene3D; 3.30.70.3270; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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 PANTHER; PTHR43100:SF2; FERREDOXIN-DEPENDENT GLUTAMATE SYNTHASE, CHLOROPLASTIC-LIKE; 1.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030428}.
FT DOMAIN 33..63
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 77..106
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 173..204
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 594 AA; 65796 MW; 11546DCFD1B5453A CRC64;
MKSILAPLKA LSFLGREPVT LPIAPRPAAP NYRGFHINDW EKCIGCGTCA TICDNYAIRM
VDIKDLSSDP IKGIKPRRPA IDYGRCCWCA LCVDVCPTGS LALSREYVHI GLDLNTFFIL
PDEKGMHGLG FPKGWAKSSD SDLLDLKRQP IPELTAKERQ DSFVEIVQGF DDQTALLEAS
RCIQCGMCHD ACPTHMHAPE YIRAIWAGEL EEAVQQIYRT NPLANVCGRV CTHRCETACS
IGVRGKAISI RWLKRYAMDK VSHERIKQIA SKGRNTIESG KKVAIVGAGP AGLTAAYDLA
RQGHAVTIFE ALEKPGGMMR YGIPEYRLPY DKIDEDIDVI ESMGVDIRCN VHIGHQMASL
ENDFDATLIA IGLHGGRSTR VPGTDHPHVY SAIDLLRRLT LKEKIEVKKK IVVIGGGNVA
FDIARSLARL QRNLFGEVKV VITALEDREN LLASPVEVKE ANEEELQLFT SRGPRRCVVK
DGTLMGLETV RCISIFDEQG RFHPKYDDSD LIFHEADMVV EAIGQAPQLD FLGDELTERL
EWDKRGRPVI NQGGCTSEPW LWAAGDVVEG PDVIHAIAAG HRVANSIHQY LSIK
//