ID A0A0S8H002_9BACT Unreviewed; 1007 AA.
AC A0A0S8H002;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=4Fe-4S dicluster domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMS25_14745 {ECO:0000313|EMBL:KPK78542.1};
OS Gemmatimonas sp. SM23_52.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703359 {ECO:0000313|EMBL:KPK78542.1, ECO:0000313|Proteomes:UP000051975};
RN [1] {ECO:0000313|EMBL:KPK78542.1, ECO:0000313|Proteomes:UP000051975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_52 {ECO:0000313|EMBL:KPK78542.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:KPK78542.1}.
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DR EMBL; LJUM01000130; KPK78542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8H002; -.
DR PATRIC; fig|1703359.3.peg.1666; -.
DR Proteomes; UP000051975; 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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd10551; PsrB; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.70.20; -; 2.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF13247; Fer4_11; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
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 Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 48..104
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 757..787
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 833..864
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 865..894
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1007 AA; 110696 MW; D4AE79C536E5FB66 CRC64;
MSEIKRRDFL KILGLSGAST GLMGCAQEPA KKLIPYLVQP EEVIPGVANW YASVCRECPA
GCGVHVKVRD GRPIKVEGNP DHPVNAGRLC ARGQAALQGL YDPDRIAGPL RRVEGRDEFE
PTTWDEAEAL LASRIRGLRR TGQAERLYLI SDGAVSSLDR LFEAWLDAVR SPNRIVHESF
DVEPLREANR LTFGRAEIPR YELDRAELIL SFGAGFLETW ISPVQYTRLF ARSQSFRDGR
KGRFVHVGPR LSLTGSNADE WVPARPASAM MLALAMTRVL VAEGRAGGRA AVLRPLVEPF
TPERVSEATG VEAEQIERLA REFADVPASL ALPPGVEMTH RNATATHVAV NLLNYAADNF
GRTVRFGPNV ARRRPADLTR WTEVIEAMRS GAVDMLLVHG SDPVHTLPPS LGLSGALENV
GLMVSFASHM DETAAHADLI LPDHTPLESW GDHEPEVGVH TLMQPTINPL FETRHTGEVL
FSLAARIGGN LGAQFLWPDY SAYLRDAWRS VQLQFAPRDD FAEFWHAAVA RGGVWREVET
QSVTLNRAVA GVEFEEPTLE GDAAARFALI AYPSPTLYDG RGANRPWLQE LPDPVTKIVW
NSWIEIHPDV ARQLEVRTGD VLAVSTPQGQ LEVPAYVYRG IRADTVAIPV GQGHTHYGRW
ARDRGVNPLA LLPGAADASS GSFAWLSTRV ALARTGRRVQ LVETQGADDD RGRAIAEVIS
LAAATEAERR ARAAEQFHSE APVEAAEDAD PKSPYRWGMA IDLSSCIGCS ACVTACYAEN
NIPVVGERRC AQGREMAWIR VERYYEHLIE EGSHGEASHG GSTQIGGGAS EDLHVVHIPM
MCQHCGNAPC EPVCPVYATY HNPEGLNVQV YNRCVGTRYC SNNCPYKARR FEWFNYEYPF
PLNLQLSPDV TVREKGVMEK CTFCVQRIMM ARSDANAQGR DVADGEVTPA CAQTCPAEAI
VFGNLRDPNS RVSQLARSGR AYHVLGELNT RPAVTYLREV AHGTEET
//
