ID A0A2S6NI44_RHOGL Unreviewed; 1024 AA.
AC A0A2S6NI44;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Tetrathionate reductase subunit A {ECO:0000313|EMBL:PPQ34271.1};
GN ORFNames=CCS01_11710 {ECO:0000313|EMBL:PPQ34271.1};
OS Rhodopila globiformis (Rhodopseudomonas globiformis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodopila.
OX NCBI_TaxID=1071 {ECO:0000313|EMBL:PPQ34271.1, ECO:0000313|Proteomes:UP000239724};
RN [1] {ECO:0000313|EMBL:PPQ34271.1, ECO:0000313|Proteomes:UP000239724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 161 {ECO:0000313|EMBL:PPQ34271.1,
RC ECO:0000313|Proteomes:UP000239724};
RX PubMed=29423563;
RA Imhoff J.F., Rahn T., Kunzel S., Neulinger S.C.;
RT "New insights into the metabolic potential of the phototrophic purple
RT bacterium Rhodopila globiformis DSM 161(T) from its draft genome sequence
RT and evidence for a vanadium-dependent nitrogenase.";
RL Arch. Microbiol. 0:0-0(2018).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
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:PPQ34271.1}.
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DR EMBL; NHRY01000120; PPQ34271.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6NI44; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000239724; 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; cd02780; MopB_CT_Tetrathionate_Arsenate-R; 1.
DR Gene3D; 2.40.40.20; -; 1.
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 InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037946; MopB_CT_Tetrathionate.
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; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000239724};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 69..144
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1024 AA; 112468 MW; D72CF53BBB0FFB52 CRC64;
MNISRRGLLA LGAVAGLGAG TIGFSRRLID LVPLRQRGRK ALHPIYGNSN TPEWLRDRAS
GQLVPNPQWT LHHTVDLQCH SECGLRVKID RKTGRIQRII GNPYHPNTLS EYTAVTTPLI
DTAALPGTVC ARGNTGIQST YDPYRVLVPL KRVGQRGSGQ WKPISWETLV TEVTEGGKIF
ADTNDPASKD MEILGFRGLY AKRNELIDPK APELGMRTNG FVLQGGRLVG TRMTFVERFV
HTFGSVNVFD HVNECELSHH IAHQHVFSGI NMTQPDVREA KFIIYWGTQP GDANFPMQTQ
GKYVAEARAK PDGLKYVVVD PKLSRGGVVG DRASWLPIRP GTDGAMAMAM IRWIIENQRY
NAPYLSYPTL AAAQSAGELS HTDSTHLVVV DPKHPQARRF LTAEVAGLGR PGATGEDDRV
VIDSASGKPA QAASVKTAQI DFAGEVNGVA VKTAFRLLKE AAEEHTIDEY AQICGIEPPR
IIELAREFTS YGRQASSTMY RGVVKHPNGY YNGVAVLLLN LLVGNMNWTG GLTAGGGGYS
VKKGPYDIDS VPEAEGLAKG VIINREKFHY EDTSEYKTQV AAGKNPYPAK RPWFPLSFAM
YTETLPSAVQ RYPYGVDILM WQKATPLYSV PGQGNPEFLD AIKDPKNIPL IIASDIIVGD
SSMFADYILP DVSHLESWDL VDTFPTTLTK GTGVRWPAVN LTSTTPDGRH VCLEEFLIDV
AKRIGMPGYG DKGIPDADGK YWPLNRREDF YLKAVANLVA AKGVGGDEVP AASPQEIEVT
ALDAFHKTYG DSLKPGEWPQ VMGCLVRGGR FQPHTGARKG DQLAYQYTKP LHFYAEKTGT
TRNSMNGEFF HGTVRWVEPA TALGKHLDAL DDPKDWPLTI ITMKGALQSH SRLASNYTLR
EITPNNGVQI AAADAQRLGI ANGDWVWVVT PEGKRRGRAV VLQGIRPGVI LFEVGYGHWG
YGATNYSVDG KRVMGDAVRR TGIHLNPIMR RDPDIWQMPL MDLAGGSVVF YNTKARLEKE
TAHA
//
