ID A0A0R2CLQ1_9LACO Unreviewed; 465 AA.
AC A0A0R2CLQ1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Lactate dehydrogenase (Oxidoreductase) {ECO:0000313|EMBL:KRM89481.1};
GN ORFNames=FD21_GL001337 {ECO:0000313|EMBL:KRM89481.1};
OS Liquorilactobacillus vini DSM 20605.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1133569 {ECO:0000313|EMBL:KRM89481.1, ECO:0000313|Proteomes:UP000051576};
RN [1] {ECO:0000313|EMBL:KRM89481.1, ECO:0000313|Proteomes:UP000051576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20605 {ECO:0000313|EMBL:KRM89481.1,
RC ECO:0000313|Proteomes:UP000051576};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM89481.1}.
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DR EMBL; AYYX01000004; KRM89481.1; -; Genomic_DNA.
DR RefSeq; WP_034995357.1; NZ_AYYX01000004.1.
DR AlphaFoldDB; A0A0R2CLQ1; -.
DR STRING; 1133569.FD21_GL001337; -.
DR PATRIC; fig|1133569.4.peg.1472; -.
DR eggNOG; COG0277; Bacteria.
DR Proteomes; UP000051576; Unassembled WGS sequence.
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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000051576}.
FT DOMAIN 45..224
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 465 AA; 50467 MW; BFE5464D21ADFCA6 CRC64;
MSVFTAYSQE EVIDELKHRA PHAEIHLDDE IAAKHAANGK AESTIDGRIL AYVAVGDKDD
IRGVLKTAIK FHLPIVPQTA DTSTVIGADG LNGGIILSLA RMNKIVEVNE DDLLAVVEPG
VINQDLDQAA RQHGLFYAPD PASKPISSIG GNVSTNAGGL SGVKYGATKD SVLGLKVMLA
NGKEIKVGGR TTKQAFGYNL TQLFVGSEGT LGIITEITLR LFPIPIGKKI YGVAFFDNMA
KLAEGVHALR ISGLYPSMLE GLDGKTVQAL DQYKQTHYAK SASSSMLIFM FDDAGETQLQ
ISQKILQEQG AWKIQITDDP AQGEKLIQLR RDMLPAVFAN GKYYIMEDMA VPSSKLAEMA
DYIVQVGDEL QVNIYTAGHA GDGNLHPTLL WNDQPQAPAN VIEATRRLFH KALDLGGTIS
GEHAVGMSKN QWNNEELGED VDVLQHQIKT LFDPMNILNP KRKIN
//
