ID A0A135VMC2_9ARCH Unreviewed; 283 AA.
AC A0A135VMC2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=AM324_16100 {ECO:0000313|EMBL:KXH73817.1};
OS Candidatus Thorarchaeota archaeon SMTZ1-83.
OC Archaea; Asgard group; Candidatus Thorarchaeota.
OX NCBI_TaxID=1706445 {ECO:0000313|EMBL:KXH73817.1, ECO:0000313|Proteomes:UP000070043};
RN [1] {ECO:0000313|EMBL:KXH73817.1, ECO:0000313|Proteomes:UP000070043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMTZ1-83 {ECO:0000313|EMBL:KXH73817.1};
RX PubMed=26824177;
RA Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT phylum with pathways for acetogenesis and sulfur reduction.";
RL ISME J. 0:0-0(2016).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|PIRSR:PIRSR006816-2};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000256|PIRSR:PIRSR006816-2};
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:KXH73817.1}.
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DR EMBL; LRSK01000182; KXH73817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135VMC2; -.
DR Proteomes; UP000070043; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd06221; sulfite_reductase_like; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43513:SF1; ANAEROBIC SULFITE REDUCTASE SUBUNIT B; 1.
DR PANTHER; PTHR43513; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT; 1.
DR Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR PRINTS; PR00371; FPNCR.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR006816-2};
KW Iron {ECO:0000256|PIRSR:PIRSR006816-2};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR006816-
KW 2}; Metal-binding {ECO:0000256|PIRSR:PIRSR006816-2}.
FT DOMAIN 11..111
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 249
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 254
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 257
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 265
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ SEQUENCE 283 AA; 32716 MW; 447F4F4DE0FCA810 CRC64;
MTETQNIENP FQPEPARIVR QYDLIKDHRF FQIRFTDMER AMSFKYKPGQ FAMLSIPGVG
EAPFSISSTP SRPGILEMGI RRTGKLTESL FRKKDNDIVF VRGPYGNGFK IEPMVERDIV
IVAGGLGVIP LRSILYYVLD NRDQFDELFF LYGARNPNEF LFRNEFFQIK DRDDIDCFYT
VDKDTTGTWT ESTGVVTKLF AKLPEIDPQT TTAVVCGPPV MYKFVIQELL KLRIPKNMIQ
MTLERRMKCG IGKCGHCALD HIYTCIDGPV FTYWDTLHFR ELI
//