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Entry: I3R806_HALMT
LinkDB: I3R806_HALMT
Original site: I3R806_HALMT 
ID   I3R806_HALMT            Unreviewed;      1049 AA.
AC   I3R806;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:QCQ76203.1};
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:AHZ23731.1};
DE   SubName: Full=Glycolate oxidase subunit GlcD {ECO:0000313|EMBL:AFK20366.1};
GN   Name=glcD1 {ECO:0000313|EMBL:AFK20366.1};
GN   OrderedLocusNames=HFX_2688 {ECO:0000313|EMBL:AFK20366.1};
GN   ORFNames=BM92_14250 {ECO:0000313|EMBL:AHZ23731.1}, C439_15219
GN   {ECO:0000313|EMBL:ELZ99221.1}, E6P09_13340
GN   {ECO:0000313|EMBL:QCQ76203.1};
OS   Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS   14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK20366.1, ECO:0000313|Proteomes:UP000006469};
RN   [1] {ECO:0000313|EMBL:AFK20366.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.2087 {ECO:0000313|EMBL:AFK20366.1};
RX   PubMed=22247127; DOI=10.1128/AEM.07114-11;
RA   Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
RT   "Identification of the haloarchaeal phasin (PhaP) that functions in
RT   polyhydroxyalkanoate accumulation and granule formation in Haloferax
RT   mediterranei.";
RL   Appl. Environ. Microbiol. 78:1946-1952(2012).
RN   [2] {ECO:0000313|EMBL:AFK20366.1, ECO:0000313|Proteomes:UP000006469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC   R-4 {ECO:0000313|Proteomes:UP000006469}, and CGMCC 1.2087
RC   {ECO:0000313|EMBL:AFK20366.1};
RX   PubMed=22843593; DOI=10.1128/JB.00880-12;
RA   Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA   Zhou J., Hu S., Xiang H.;
RT   "Complete genome sequence of the metabolically versatile halophilic
RT   archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT   hydroxyvalerate) producer.";
RL   J. Bacteriol. 194:4463-4464(2012).
RN   [3] {ECO:0000313|Proteomes:UP000011603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC   R-4 {ECO:0000313|Proteomes:UP000011603};
RA   Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA   Eisen J.A., Facciotti M.T.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ELZ99221.1, ECO:0000313|Proteomes:UP000011603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 {ECO:0000313|EMBL:ELZ99221.1}, and ATCC 33500 / DSM
RC   1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC   {ECO:0000313|Proteomes:UP000011603};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [5] {ECO:0000313|EMBL:AHZ23731.1, ECO:0000313|Proteomes:UP000027075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 {ECO:0000313|EMBL:AHZ23731.1}, and ATCC 33500 / DSM
RC   1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC   {ECO:0000313|Proteomes:UP000027075};
RA   Bautista V.;
RT   "Transcriptional profiles of Haloferax mediterranei on the basis of
RT   nitrogen availability.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:AFK20366.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.2087;
RA   Wang L., Yang H., Xiang H.;
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:QCQ76203.1, ECO:0000313|Proteomes:UP000299011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 {ECO:0000313|EMBL:QCQ76203.1}, and ATCC 33500 / DSM
RC   1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC   {ECO:0000313|Proteomes:UP000299011};
RA   DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA   Roberts R.J.;
RT   "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT   mediterranei.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP001868; AFK20366.1; -; Genomic_DNA.
DR   EMBL; CP007551; AHZ23731.1; -; Genomic_DNA.
DR   EMBL; AOLO01000012; ELZ99221.1; -; Genomic_DNA.
DR   EMBL; CP039139; QCQ76203.1; -; Genomic_DNA.
DR   RefSeq; WP_004060167.1; NZ_CP039139.1.
DR   AlphaFoldDB; I3R806; -.
DR   STRING; 523841.HFX_2688; -.
DR   PaxDb; 523841-HFX_2688; -.
DR   GeneID; 40157419; -.
DR   KEGG; hme:HFX_2688; -.
DR   PATRIC; fig|523841.21.peg.3072; -.
DR   eggNOG; arCOG00337; Archaea.
DR   HOGENOM; CLU_010756_0_0_2; -.
DR   OrthoDB; 2837at2157; -.
DR   Proteomes; UP000006469; Chromosome.
DR   Proteomes; UP000011603; Unassembled WGS sequence.
DR   Proteomes; UP000027075; Chromosome.
DR   Proteomes; UP000299011; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster 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   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
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; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
FT   DOMAIN          73..309
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1049 AA;  114330 MW;  4118ACF64444CC75 CRC64;
     MVGDDSSWPN RATTAVDEGD LSDFRRFQES RDYEVSDVAA HAELASDLRD AVEGEVRFDE
     YTQVLYATDG SIYRARPAGV VIPRDPDDVR AAVEIAVAHD VPILPRGAGS SLAGQTVGPG
     CVVLDFSKYM DDIVAVDPEN RRATVQPGVV QDDLDDRLSA HGLKFAPDPA SSNRATIGGG
     IGNNSTGAHS VRYGITDAYT EELRVVLADG SLMHTRDVVV GSDEWDDIVA KDDREAEIYR
     TVVRLVEENE TEIEQRYPEL KRCVSGYNLH KVVFENDDGE TVVNLSKLFV GAEGTLGVVV
     EATVSLVTVP EETALVLYAY DDLLDAMTAV PDALDFDASA VELMDDEVFR MAAESSEYAQ
     YVEGIPDGTA ATLMLEFDSE LHDDFEAVIQ AANDHFLRSE SKAEAESKAE AELKSEADDG
     RAFDAIEAYT DEAQANLWKL RKAAIPLLMS LQGDPKPYPF IEDASVPPEE LAEYVQSFED
     VLADHGTSAA YFAHAGAGTL HIRPILNLKD RDGIETMRSI TDDVTDLVLE HHGAFSGEHG
     DGLARTEWNP KMYGPALWDA FKQVKSAFDP DWRMNPGKVV YRSDDPTDMR ENLRYGASYA
     SLEPATTLEF EDEGGFSHLV ELCNGCGTCR QTGSETMCPT YRASKDEAET TRGRANMLRA
     AISGDLPEEE LYTDRFQEEI LGLCIGCKGC KNDCPTGVDL AKLKAEVKHK HHAEAGASIR
     ERLFANIDRF ARLGSVLAPV SNWAAELPGA RDAMDRLVGI ASDRELPSFT SNTLEQWMKF
     REATVSQAEA THRVLLFPDT YTNYVTPEIG KAAVRTLEAA GVHVQLAENV HPSGRAAYSG
     GFLDLARKRA GHNVEALRPF VEDGWSVVFT EPSDVVMFQD EYDDLLPNEA VAPVGAAAYG
     VMEFIDVYRL DEEFPIRGRE STGLGSVGTA GTAVADGGEF GSLTYHGHCN QKALNKDHHA
     VGVLRRVGYD VDPLNSGCCG MAGSFGYESE HYDLSKAIGR ILFEKVDESE ADTVVAPGAS
     CRSQLAERER EGVHRPAHPI EKVAAALAG
//
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