ID B9M1Q0_GEODF Unreviewed; 461 AA.
AC B9M1Q0;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=D-lactate dehydrogenase, flavoprotein subunit, putative {ECO:0000313|EMBL:ACM19196.1};
GN Name=larD {ECO:0000313|EMBL:ACM19196.1};
GN OrderedLocusNames=Geob_0834 {ECO:0000313|EMBL:ACM19196.1};
OS Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS daltonii).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM19196.1, ECO:0000313|Proteomes:UP000007721};
RN [1] {ECO:0000313|EMBL:ACM19196.1, ECO:0000313|Proteomes:UP000007721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC {ECO:0000313|Proteomes:UP000007721};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kostka J., Richardson P.;
RT "Complete sequence of Geobacter sp. FRC-32.";
RL Submitted (JAN-2009) 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; CP001390; ACM19196.1; -; Genomic_DNA.
DR RefSeq; WP_012645925.1; NC_011979.1.
DR AlphaFoldDB; B9M1Q0; -.
DR STRING; 316067.Geob_0834; -.
DR KEGG; geo:Geob_0834; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_7; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000007721; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
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; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR42934:SF3; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007721}.
FT DOMAIN 36..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 461 AA; 50154 MW; 573F6AE245C2F459 CRC64;
MLESRILDQL KTIVGSENVA TERQDLLCYG YDATQMEFLP DAVVHPGSVD EISQILNLAN
AENIHVFPRG AGSGFTGGAL PKGGGIVLVV TRLNRILRID TENLIAEVEP GVVTEQFQME
VEKLGLFYPP DPASLKFSTL GGNVAENAGG PRCVKYGVTR DFVMGLEVVL PTGDIIRTGG
ETYKGVVGYD LTRLLCGSEG TLGIITKIIF KLLPLPEAKK TMLTIFDSID GAARAVSTII
GNKIIPTTLE FMDHATLQCV EKRFNLGIPE IGRAVLIIEV DGDRELIETQ AARIQELVRP
LGLVECKVAK DAAESEALWK VRRLVSPSLR DVNPDKFNED IVVPRSKVPD VIRRIEKIQQ
RYDIPIVNFG HAGDGNIHVN VMIDKTVPGM EEKAHQAIGE VFQAALDLNG TMSGEHGVGL
AKQPYIHLEL KGAQLAAMQA IKKALDPKNI LNPGKMFPVK S
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