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Database: UniProt
Entry: V4XL11_9ARCH
LinkDB: V4XL11_9ARCH
Original site: V4XL11_9ARCH 
ID   V4XL11_9ARCH            Unreviewed;       766 AA.
AC   V4XL11;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Fe-S oxidoreductase {ECO:0000313|EMBL:ESS09044.1};
GN   ORFNames=A07HN63_01254 {ECO:0000313|EMBL:ESS09044.1};
OS   uncultured archaeon A07HN63.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=1412873 {ECO:0000313|EMBL:ESS09044.1, ECO:0000313|Proteomes:UP000030667};
RN   [1] {ECO:0000313|Proteomes:UP000030667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24335829;
RA   Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S.,
RA   Heidelberg K.B., Banfield J.F., Allen E.E.;
RT   "Seasonal fluctuations in ionic concentrations drive microbial succession
RT   in a hypersaline lake community.";
RL   ISME J. 0:0-0(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; KI543214; ESS09044.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4XL11; -.
DR   STRING; 1412873.A07HN63_01254; -.
DR   PATRIC; fig|1412873.3.peg.1348; -.
DR   Proteomes; UP000030667; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02754; CCG; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
FT   DOMAIN          413..445
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          741..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..759
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   766 AA;  83364 MW;  70EF5E73BB7F9FDC CRC64;
     MRNVSGYNLD KLVADAEEHG AVNVGRLLAG SEGTLGVVTE ATVSLEPIPN ETAVVMLTYD
     DVLDAMEDVA PILDHDPAAV EVLDDVFLDL AADRPEFADV VDILPEGTDS TLLVEFYADS
     MADGKQKIAD LLADRLPSVD AAVEPSNGDG AGEKTTDETY AVDALEAYDA DRQTKFWKMR
     KAGLPILLSR TSDEKHWPFI EDTAVPAENL PEYVADIQAL FDEYDTFASY YAHAGPGVLH
     IRPLLDLKAD DGIETMHEIC DDVTDLVIEY GGSVSGEHGD GRARTTWNRK LYGSEIWSLF
     QRLKAAFDPD DRLNPGNVSG DADPTENLRY DADYEFDAGF EPTLNWDNEN GFQGMTELCH
     GCAGCTGHQD TTGSVMCPTY RATENEEITS TRGRANMLRQ SMSGDLPDDV FSEEFSHEVL
     DLCIGCKGCK RDCPSGVDMA KLKTEVAHER HQREGVALRD RLFANVETLY SLGSSLAPLS
     NWATKLPGSG LLAEKTLGIA RERELPTFSR TTLQQWDRGR TPAVSEREAD RQALLIADPY
     TNYTQPEVGK AAVRTLEAAG VHVEIADEVT DSGRPAHSKG LLDQSKATAE ANVEVLGDRV
     AEGWDLVSVE PSDAVMYQDD YLDLLSGEAV EAVADNTYSV LEYIDTFRLD DALDTTASDE
     LAYHGHCHQT AASREHHAVG VLRRAGYEVD VLDTTCCGMA GSFGYEAEHY SMSQAIGDLL
     FDAVDDSPAA EVVAPGTSCR SQLGDTDRYD GKPAHPVEKV ADALVD
//
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