ID R1G1I9_BOTPV Unreviewed; 736 AA.
AC R1G1I9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Putative lipoate-protein ligase A {ECO:0000256|ARBA:ARBA00015925};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=UCRNP2_7993 {ECO:0000313|EMBL:EOD45290.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD45290.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
CC -!- FUNCTION: Catalyzes both the ATP-dependent activation of exogenously
CC supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl
CC onto the lipoyl domains of lipoate-dependent enzymes.
CC {ECO:0000256|ARBA:ARBA00003253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = AMP +
CC diphosphate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier
CC protein]; Xref=Rhea:RHEA:49288, Rhea:RHEA-COMP:10500, Rhea:RHEA-
CC COMP:10502, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:83088, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:456215; EC=6.3.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00043803};
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005124}.
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00005085}.
CC -!- SIMILARITY: Belongs to the LplA family.
CC {ECO:0000256|ARBA:ARBA00008242}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KB916622; EOD45290.1; -; Genomic_DNA.
DR RefSeq; XP_007587236.1; XM_007587174.1.
DR AlphaFoldDB; R1G1I9; -.
DR STRING; 1287680.R1G1I9; -.
DR KEGG; npa:UCRNP2_7993; -.
DR eggNOG; KOG1339; Eukaryota.
DR eggNOG; KOG3159; Eukaryota.
DR HOGENOM; CLU_376823_0_0_1; -.
DR OrthoDB; 3087283at2759; -.
DR Proteomes; UP000013521; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd16443; LplA; 1.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR12561; LIPOATE-PROTEIN LIGASE; 1.
DR PANTHER; PTHR12561:SF3; LIPOYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..736
FT /note="Putative lipoate-protein ligase A"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004350937"
FT DOMAIN 90..399
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 467..675
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT REGION 407..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 121..126
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 736 AA; 79130 MW; D3947799B8FF67B7 CRC64;
MLSSRLLASA AAAYLALPPA AAFYPYALED ASLLAARHEP AVSSAQDQSF AVPIRRTPTR
RDNQFNVVTA NDPTQSDSVA VDSDGSDFSY FSTVKFGSSD VEYYLLLDSG AANTWVMSAD
CTTDSCAKHS TLGPSGSSTL EVTSNTFSIA YGTGNVNGTL ASDKVHVSSF SVDLTFGLAD
FASPEFASYP MDGILGLGRA DRTDNDVTDG TLLDALAEAS LIPAKLYGIH LSRNSDGLKD
GELNLGAPNP DRYDGDLAWT STIDNDRGFW EIPIDDAAYG GTQAGLTDRT AIIDTGTSYM
LLPGNDAAAL HKLIPQSAQN GEIFTIPCST TQSLQLSFNN IAYNISAKDY VGRNVGGSTC
QSNIIGRRTF GDKQWLVGAV FLKNVYAVFD YDNSRIGFGV KGSGSSMAET SASPTSTSAA
GSTSVKSHTT INRTNLRPAA KLHAFVSRSR DPLVNLSIEH YLLQKSAPDS VVLFLYTNRP
CIVIGRNQNP WLEVNLALLR RGQVDLVRRR SGGGTVFHDE GNVNWTVISP PATFTRDKHA
EMVVHALRQL AVERARVNER HDIVLDQGSR ASAALQADTH RTPFTVDDPA GPRPLKVSGS
AYKLVRGRAL HHGTCLLCSP NLTIIPQYLR SPAKPFIKAH GVESVSSPVA NIGIDTSAFI
QAVQREFARM YGSASAMEVG DEQLRLPELR KGYDEMRTLD WTYLQTPKFT FSVPAADPVP
QENTALPAGF SPSASK
//
