ID A0A0J1FHW6_9FIRM Unreviewed; 1040 AA.
AC A0A0J1FHW6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Tetrathionate reductase subunit A {ECO:0000313|EMBL:KLU63079.1};
DE EC=1.8.-.- {ECO:0000313|EMBL:KLU63079.1};
GN Name=ttrA {ECO:0000313|EMBL:KLU63079.1};
GN ORFNames=CEB3_c05730 {ECO:0000313|EMBL:KLU63079.1};
OS Peptococcaceae bacterium CEB3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=999898 {ECO:0000313|EMBL:KLU63079.1, ECO:0000313|Proteomes:UP000035957};
RN [1] {ECO:0000313|EMBL:KLU63079.1, ECO:0000313|Proteomes:UP000035957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEB3 {ECO:0000313|EMBL:KLU63079.1,
RC ECO:0000313|Proteomes:UP000035957};
RA Poehlein A., Petzsch P., Johnson B.D., Schloemann M., Daniel R.,
RA Muehling M.;
RT "Genome sequence of the moderately acidophilic sulfate reducing
RT Peptococcaceae bacterium strain CEB3.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KLU63079.1}.
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DR EMBL; LDXJ01000032; KLU63079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1FHW6; -.
DR STRING; 999898.CEB3_c05730; -.
DR PATRIC; fig|999898.3.peg.686; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000035957; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
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; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KLU63079.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035957};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..130
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1040 AA; 114139 MW; 2159CB05832F7201 CRC64;
MSDTLNMQRR TFLKGVALGG SLLGGLWGSM PWLPDVVKQR GQYVYPQRVE SWPGVDVRYS
VCRQCRSDCG LEARVFNNVL LKLDGNPYHP NSTEPQLPYA TDPQEAVRVK IPHSICARGQ
AGAQTLYDPY RVLQPLKRIG PRGSGKFKTI SWEQLIEETV NGGLLFKDVP GEEKRRVEGF
AQLWNQGRGR FTPADPAHPD MGPQTNELVM YWGRAEVGQN TFIQRFATAF GSVNALPHVG
ICELNHHVAT QQSLNGAVAM LKPDIANSEF IIWFGAGIYT ANFPMQALAR KIAAASSKGL
KFVLVDVSAT AGVAHADRFI TVKPGGDGAL AMGMVRWILE NHRYDSRFLM NTTLKAAQAQ
GEPNYANAAY LVISDPSHPK AHKFARAADV GLAAAGSADA DKYVVVDAGG QAAVFDTVAQ
GLLWPQGDLE VKPVTVGGVS CLTAMQILYQ TAQEHTLADY AKLAGVSTQV ITELAREFTS
HGKKAVADFY RGPAMHTNGF YNGRSIMTLN FLIGNIDWAG GYMAGGGTAD FMGAKPTSPF
HLGKWPNQPK GVPNGVKISR EGAFYEKTTY YKELKNEGRS PFPAKRPWYP FGFGIWHEIF
GGIWDAYPYP AKIVYQHMGN PAYSAPPGMG GADDEKLPWF RMIKDLDKVP LFITDDIVLS
ETSMYADYIV PDSTFLEAWG ALPGFPTTPT SVIGIRQPIV DPLMAKTKDG RPMCFETYYI
DVAEKLGMPG FGKNAFMDGG SLHRREDFYL RMIANVAYDA GTYLQLDSLG QPAKMGPVPD
ATAAEMQSVA RWQKQFGSVL TPAQWRKVAY VMARGGRFED YGLAYLGDKP GWLTHRYGSA
KNLLQIYNEG VGSTHNAISG EIFHGTGIAL PQRTLKGRLL DEIDSSKEFN FHLTTYKLPI
HTQSRTINDP WLLELLAQNY IELNDADAKR LGIADGDWIR VASASYPRGI TGKVRSLPGV
RPGVVTFTNS FGHWHYGSGS WQVDGQTLQG DDSRNGGVRL NPLMRLDPDM QDASGWGTCL
EDPVGGGASY FDTKVKISKV
//
