ID F8D7U7_HALXS Unreviewed; 543 AA.
AC F8D7U7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:AEH36678.1};
GN OrderedLocusNames=Halxa_2053 {ECO:0000313|EMBL:AEH36678.1};
OS Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halopiger.
OX NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH36678.1, ECO:0000313|Proteomes:UP000006794};
RN [1] {ECO:0000313|EMBL:AEH36678.1, ECO:0000313|Proteomes:UP000006794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18323 / JCM 14033 / SH-6
RC {ECO:0000313|Proteomes:UP000006794};
RX PubMed=22675596; DOI=10.4056/sigs.2505605;
RA Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A.,
RA Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N.,
RA Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Halopiger xanaduensis type strain (SH-6(T)).";
RL Stand. Genomic Sci. 6:31-42(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002839; AEH36678.1; -; Genomic_DNA.
DR RefSeq; WP_013879571.1; NC_015666.1.
DR AlphaFoldDB; F8D7U7; -.
DR STRING; 797210.Halxa_2053; -.
DR GeneID; 10797015; -.
DR KEGG; hxa:Halxa_2053; -.
DR eggNOG; arCOG02233; Archaea.
DR HOGENOM; CLU_008878_4_1_2; -.
DR OrthoDB; 346033at2157; -.
DR Proteomes; UP000006794; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS00221; MIP; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006794}.
FT DOMAIN 210..239
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 59268 MW; 83DD70132C4EE329 CRC64;
MNGDRPPAES AEPVDDIDRT PVPDADVCVI GAGPAGGLVA DRLADAGHEV VVLEAGPRFD
SEDRLARQER AIRPAYDRPD VWDGDPERDA HSASGEWYYP LNHARVKGVG GSTLHWQGMV
MRLHEDDFNS ESARGVGTDW PIDYPDLRPY YAEAERELGV AGASDNPFAP PREEPHPMPA
FEPSYSDSLF AEACEEVGVA MHSVPNARNS EAYDDRSACV GYGTCQPVCP AGAKYDATVH
VERAESKGTT VIDRAPVQRL EHGADRIEAA VYATPEDEEQ RQEADAFVVA CGGVETPRLL
LLSESSDYPD GLANSSGLVG QFFMDHLFAG TGGVLDERTR QNHVGFLTSE SHQFYDEADD
EYAPFKLEFF NYDGPSPVEM ALTGEDWGDD LLERLGSEYG NHIGMGALVE QLPREDSYVG
LDRSTTDDRG NPVPDVHWNV GDRALRTIER VNEIQERILE ELGAEITWQV GPDNTGPAYH
HMGTTRMGDD PAESVVNARL RTHDLENCWI ASSSVFPTAG AMNPTLTIAA LALKAADHVH
GNL
//