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Database: UniProt
Entry: F2R4U7_STRVP
LinkDB: F2R4U7_STRVP
Original site: F2R4U7_STRVP 
ID   F2R4U7_STRVP            Unreviewed;       455 AA.
AC   F2R4U7;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Fe-S protein lactate dehydrogenase {ECO:0000313|EMBL:CCA55968.1};
GN   OrderedLocusNames=SVEN_2682 {ECO:0000313|EMBL:CCA55968.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA55968.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA55968.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC   PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; FR845719; CCA55968.1; -; Genomic_DNA.
DR   RefSeq; WP_015033886.1; NZ_JABVZO010000616.1.
DR   AlphaFoldDB; F2R4U7; -.
DR   STRING; 953739.SVEN_2682; -.
DR   GeneID; 69864816; -.
DR   KEGG; sve:SVEN_2682; -.
DR   PATRIC; fig|953739.5.peg.4872; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_9_1_11; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000006854; 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; 3.30.70.2740; -; 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; 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; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   PANTHER; PTHR42934:SF2; 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:UP000006854}.
FT   DOMAIN          36..215
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   455 AA;  47699 MW;  2A400407D2571504 CRC64;
     MDDLLTRLRA GLPAEALLTD PDVTASYAND MASFCESGAP AVVVLPRTVE QVRHVMRTAT
     ELRVPVVPQG ARTGLSGGAN ASEGCIVLSL VKMDRILEIN PVDRIAVVEP GVINAVLSRA
     VAEHGLYYPP DPSSWEMCTI GGNIGTASGG LCCVKYGVTA EYVLGLDVVL ADGRLLTTGR
     RTAKGVAGYD LTRLFVGSEG SLGIVVRAVL ALRPQPPAQL ALAAEFPSSA AACEAVCAIM
     ERGHTPSLLE LMDRTTVQAV NKLARMGLPD TTEALLLCAF DTPDPAADLA AVGELCKAAG
     ATEVVPAADT AESELLLQAR RLSLTALETI KSATMIDDVC VPRTRLAEML DGTAAVARKY
     GLTIGVCAHA GDGNTHPVVC FDHTDEDESR RARESFDEIM ALGLALGGTI TGEHGVGVLK
     KDWLARELGP VGLELQRGIK ATFDPLGLLN PGKLF
//
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