UniProt: L0AGU8

Database: UniProt
Entry: L0AGU8_NATGS

LinkDB:  L0AGU8_NATGS 
Original site:  L0AGU8_NATGS

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Ontology (2)   
   GO (2)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (17)   
   InterPro (10)   
   Pfam (4)   
   PROSITE (3)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   L0AGU8_NATGS            Unreviewed;      1022 AA.
AC   L0AGU8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=D-lactate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:ELY64223.1};
DE   SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:PLK20293.1};
DE   SubName: Full=FAD/FMN-dependent dehydrogenase {ECO:0000313|EMBL:AFZ72392.1};
GN   OrderedLocusNames=Natgr_1166 {ECO:0000313|EMBL:AFZ72392.1};
GN   ORFNames=C490_14580 {ECO:0000313|EMBL:ELY64223.1}, CYV19_10020
GN   {ECO:0000313|EMBL:PLK20293.1};
OS   Natronobacterium gregoryi (strain ATCC 43098 / DSM 3393 / CCM 3738 / CIP
OS   104747 / IAM 13177 / JCM 8860 / NBRC 102187 / NCIMB 2189 / SP2).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronobacterium.
OX   NCBI_TaxID=797304 {ECO:0000313|EMBL:AFZ72392.1, ECO:0000313|Proteomes:UP000010468};
RN   [1] {ECO:0000313|Proteomes:UP000010468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43098 / CCM 3738 / NCIMB 2189 / SP2
RC   {ECO:0000313|Proteomes:UP000010468};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Natronobacterium gregoryi SP2.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFZ72392.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SP2 {ECO:0000313|EMBL:AFZ72392.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Natronobacterium gregoryi SP2.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ELY64223.1, ECO:0000313|Proteomes:UP000011613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP2 {ECO:0000313|EMBL:ELY64223.1,
RC   ECO:0000313|Proteomes:UP000011613};
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   [4] {ECO:0000313|EMBL:PLK20293.1, ECO:0000313|Proteomes:UP000234484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP2 {ECO:0000313|EMBL:PLK20293.1,
RC   ECO:0000313|Proteomes:UP000234484};
RC   TISSUE=Freeze-dried powder thallus {ECO:0000313|EMBL:PLK20293.1};
RA   Jiang L., He B., Kang J., Yu M., Li N., Fang Y., Tang Z., Wu P., Yao P.,
RA   Huang J.;
RT   "The characterization of oligonucleotides binding to NgAgo.";
RL   Submitted (DEC-2017) 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; CP003377; AFZ72392.1; -; Genomic_DNA.
DR   EMBL; AOIC01000109; ELY64223.1; -; Genomic_DNA.
DR   EMBL; PKKI01000028; PLK20293.1; -; Genomic_DNA.
DR   RefSeq; WP_005580632.1; NZ_PKKI01000028.1.
DR   AlphaFoldDB; L0AGU8; -.
DR   STRING; 797304.Natgr_1166; -.
DR   GeneID; 14207034; -.
DR   KEGG; nge:Natgr_1166; -.
DR   PATRIC; fig|797304.7.peg.2955; -.
DR   eggNOG; arCOG00337; Archaea.
DR   HOGENOM; CLU_010756_0_0_2; -.
DR   Proteomes; UP000010468; Chromosome.
DR   Proteomes; UP000011613; Unassembled WGS sequence.
DR   Proteomes; UP000234484; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 2.
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; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
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; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000010468}.
FT   DOMAIN          58..302
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          669..700
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1022 AA;  110623 MW;  93BA828D7772CB44 CRC64;
     MSLESSADPA TDRRASYDYR SDDIDRPALV ADLETLVDCD VRADSYSRQL YATDASIYEL
     TPIAVVFPES TDDVAAVLEY CSERRIPVLP RGGGTSLAGQ AVNRAVVLDF IRQMNEILAI
     DPDEGAATVQ AGTVIETLNE ALASHDLKFA PDPAWGDKSA IGGAIGNNST GAHSLQYGKT
     DAYVESAEVV LADGTVTEFG EVTLEEVDDR ADSDGDLEGR IYAAVRRVVD EKGDLVDETY
     PDRKRNVSGY NLDRLVAEAR GDALPGGEET GDPGTVNLAR LLAGSEGTLA VVTEVTVSLT
     PVPETKAVSL LCYRDLHDAM EDVAPILEHD PAAVEVLDGV LLDLACDTAE FASVTERLPD
     RTNAVLLVEF YAEDGDHGRE QVAGLLADRC PDATAAGEPA DDAPVLEAGE RAIDGLEAYD
     DAERAKLWKL RKSGLPILLS RTTDEKHVSF IEDTAVPPEN LPTFVERFEA ILDDHDTYAS
     FYAHAGPGVL HVRPLINTKT EAGLEQLHGI ADDVTDLVVE LDGAVSGEHG DGRARTQWNR
     KRYGEELWET FQDVKTAFDP DWILNPGQIV FREQNPTDLR ENLRFDPEYE FDAGFEPTLE
     WNNDNGFQGM VELCHGCGGC RGEQSTTGGV MCPTYRASKE ESTSTRGRAN ALRQAMSGDL
     EPGEAFTDEF VEEVMELCIG CKGCAIDCPS EVDMAKLKAE VTHEYVERNG TTLRDRLFAN
     VHALSRLGSR FAPLSNVLPR VPGARWLLEA TLGIDSSRPL PTFYGETFRD WFDERGGATV
     PETAAERKAI VYPDTYTNYS NPDAGKATVR VLEAAGVHVT VPDELGDTGR PAFSKGFLEQ
     ARETAVGNVE HLAPQVTNGW DVVVVEPSDA VMLQSDYLDL LDDDAVEALA ASTYGACEYV
     DTFQLDESIT FDVVDEDLTY HGHCHQKATA KDHHAVGVLR RAGYAVESLD SGCCGMAGSF
     GYEAEHGSMS DAIASILYDQ VANSDGDRVV APGASCRTQL ENRPGGENPP TPIEVAAEAL
     EE
//

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