ID A0A2P6V675_9CHLO Unreviewed; 1329 AA.
AC A0A2P6V675;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Dihydrolipoyl dehydrogenase {ECO:0000313|EMBL:PSC69589.1};
GN ORFNames=C2E20_6828 {ECO:0000313|EMBL:PSC69589.1};
OS Micractinium conductrix.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Micractinium.
OX NCBI_TaxID=554055 {ECO:0000313|EMBL:PSC69589.1, ECO:0000313|Proteomes:UP000239649};
RN [1] {ECO:0000313|EMBL:PSC69589.1, ECO:0000313|Proteomes:UP000239649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 241.80 {ECO:0000313|EMBL:PSC69589.1,
RC ECO:0000313|Proteomes:UP000239649};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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:PSC69589.1}.
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DR EMBL; LHPF02000025; PSC69589.1; -; Genomic_DNA.
DR STRING; 554055.A0A2P6V675; -.
DR Proteomes; UP000239649; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR22912:SF151; DIHYDROLIPOYL DEHYDROGENASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR Pfam; PF03031; NIF; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; Membrane {ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000239649};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 105..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 996..1015
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1206..1224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1244..1269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1281..1299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 190..332
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 401..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1329 AA; 141241 MW; 6D5E39292737CB8B CRC64;
MLRQAVAGWR SVQRRAADDA RAKLQRAFSD APPPGSRSRL NALTEESETA HKLFDNARLP
PELTEAAAAG GGTAQAAGGA AGVAAADAAA LEALESSAVG RAFSVLGNVL FFGGVAAASF
FGYYTYSYNC DQLDRMVAET ESKAENTFVG SSVWVPVMRW YSEQRRHLEG EMKKYADPPS
DRLLPDLPPN AHHIKTLVLD LDDVLVHSDW TRGRGWRTFK RPGVEDFIKS MAQYYELVVY
TSQLPTYADP ILDRLDPQRL IQYRLYRDST QYVNGRHVRD LSKLNRDMRQ VMFITADKDA
YQLQPENAVK LSKEWKEGDT MLLDLLPFLE AVVRTQVPDV RDVVKSYDGQ DIPTAFRERM
KRVQESQAAR QQTGKGFLGG RARRAARLGF APRIAGQRIA AASAKPSRPS AVPAARRVAR
AQASGKNGAP GAASSSSSGE YDYDLIIIGC GVGGHGAALH AVECGLKVAI VEGHEIGGTC
VNRGCVPSKA LLAASNEVRK LRNDHHHKTL GIQLAGAATF DRQAIADHAI NLAATVQTNL
QRSLESLGVT ILRGQAKLTG SHSITYGLPG RVDVGGSATA RDIIISTGSV PFVPGGIEVD
GKTVFTSDHA LKMEWLPNWI AIIGSGYIGL EFSDVYTALG CEVTFVEALP NIMPGFDKEI
AKLAQRLLIN SRPIDFHTNV IASKVTPGVP GVKPVKIELT DFTTKEVVDE LEVDACLVAT
GRAPYTNGLN LPAVNVATDR RGFVPVNDKM EVLDKDGKVV PHLYCIGDAN GKYMLAHAAS
AQGIAAVECI CGRERAVNHL AVPAACFTHP EVSFVGLTED AVHEKAEKEG WADKLGVSKT
YYKANSKSLA ELESDGMAKL MYRKDTGQIF GVHMIGLHSA DNIHEFSNAM NMGMTLRDLK
FNVHAHPTVA EVNEELIRHA VLENVGSVKP AAAKQPVAAL SHSLGRRDVA TARSQAALNL
TACLALGGAT AAALLAGRRQ LLGLLRLEPA LLAEALLFWT LLAAVMPCTL ANLAVSGILQ
AAAAAAAGSS APTEAEPAAA AAAAAAGGEG SGAVEADMLA PLLAAECSTA AGGAPTQPGG
SQPRRWQRLA SLQAELLAAL SWHHVSALTR DAANVAARAL VVQGSTFLTA VAAARLGAAP
LAAHHIATTL WVLPCHLIAG LQTAALVLGG RLAGTALARG GDGLPDVLHS EEVSPRRLWR
RLVRRLVLFS ACLGTAVAAC YLAAQRPLIV LFTSDADVAG QLATPVWPAM CLLVLLFAPT
MTLTGLIFAA QLFAYMRCLQ LLGFGLVFCP ALWAATALAP GSLPALWAAK LAFYVWQLAA
EAAGVASTY
//
