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Database: UniProt
Entry: A0A085I3V8_9ENTR
LinkDB: A0A085I3V8_9ENTR
Original site: A0A085I3V8_9ENTR 
ID   A0A085I3V8_9ENTR        Unreviewed;       338 AA.
AC   A0A085I3V8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   22-NOV-2017, entry version 26.
DE   RecName: Full=Lipoate-protein ligase A {ECO:0000256|HAMAP-Rule:MF_01602};
DE            EC=6.3.1.20 {ECO:0000256|HAMAP-Rule:MF_01602};
DE   AltName: Full=Lipoate--protein ligase {ECO:0000256|HAMAP-Rule:MF_01602};
GN   Name=lplA {ECO:0000256|HAMAP-Rule:MF_01602,
GN   ECO:0000313|EMBL:KFD02904.1};
GN   ORFNames=GKAS_02476 {ECO:0000313|EMBL:KFD02904.1};
OS   Kluyvera ascorbata ATCC 33433.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Kluyvera.
OX   NCBI_TaxID=1006000 {ECO:0000313|EMBL:KFD02904.1, ECO:0000313|Proteomes:UP000028600};
RN   [1] {ECO:0000313|EMBL:KFD02904.1, ECO:0000313|Proteomes:UP000028600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33433 {ECO:0000313|EMBL:KFD02904.1,
RC   ECO:0000313|Proteomes:UP000028600};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction
RT   of the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes both the ATP-dependent activation of
CC       exogenously supplied lipoate to lipoyl-AMP and the transfer of the
CC       activated lipoyl onto the lipoyl domains of lipoate-dependent
CC       enzymes. {ECO:0000256|HAMAP-Rule:MF_01602,
CC       ECO:0000256|SAAS:SAAS00894010}.
CC   -!- CATALYTIC ACTIVITY: ATP + (R)-lipoate + a [lipoyl-carrier
CC       protein]-L-lysine = a [lipoyl-carrier protein]-N(6)-(lipoyl)lysine
CC       + AMP + diphosphate. {ECO:0000256|HAMAP-Rule:MF_01602,
CC       ECO:0000256|SAAS:SAAS00603726}.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01602, ECO:0000256|SAAS:SAAS00701662}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01602,
CC       ECO:0000256|SAAS:SAAS00894007}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01602,
CC       ECO:0000256|SAAS:SAAS00894009}.
CC   -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group
CC       of lipoic acid is attached via an amide linkage to the epsilon-
CC       amino group of a specific lysine residue of lipoyl domains of
CC       lipoate-dependent enzymes. {ECO:0000256|HAMAP-Rule:MF_01602}.
CC   -!- SIMILARITY: Belongs to the LplA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01602, ECO:0000256|SAAS:SAAS00894016}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KFD02904.1}.
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DR   EMBL; JMPL01000044; KFD02904.1; -; Genomic_DNA.
DR   RefSeq; WP_035894566.1; NZ_JMPL01000044.1.
DR   EnsemblBacteria; KFD02904; KFD02904; GKAS_02476.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000028600; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016979; F:lipoate-protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01602; LplA; 1.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR023741; Lipoate_ligase_A.
DR   InterPro; IPR019491; Lipoate_protein_ligase_C.
DR   InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR   PANTHER; PTHR12561; PTHR12561; 1.
DR   PANTHER; PTHR12561:SF5; PTHR12561:SF5; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF10437; Lip_prot_lig_C; 1.
DR   TIGRFAMs; TIGR00545; lipoyltrans; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01602,
KW   ECO:0000256|SAAS:SAAS00428641};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028600};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01602,
KW   ECO:0000256|SAAS:SAAS00894000};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01602,
KW   ECO:0000256|SAAS:SAAS00603725, ECO:0000313|EMBL:KFD02904.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01602,
KW   ECO:0000256|SAAS:SAAS00026749};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:KFD02904.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028600};
KW   Transferase {ECO:0000313|EMBL:KFD02904.1}.
FT   DOMAIN       29    216       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
FT   NP_BIND      76     79       ATP. {ECO:0000256|HAMAP-Rule:MF_01602}.
FT   BINDING      71     71       ATP. {ECO:0000256|HAMAP-Rule:MF_01602}.
FT   BINDING     134    134       ATP. {ECO:0000256|HAMAP-Rule:MF_01602}.
FT   BINDING     134    134       Lipoate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01602}.
SQ   SEQUENCE   338 AA;  38054 MW;  F695F0F5C3630435 CRC64;
     MSTLRLLLSD SHDPWFNLAV EECIFRQMPA TQRVLFLWRN ADTVVIGRAQ NPWKECNTRR
     MEEDNVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTI STSIVLEALN SLGITAEASG
     RNDLIVKTEE GDRKVSGSAY RETKDRGFHH GTLLLNADLS RLANYLNPDK KKLQAKGITS
     VRGRVANLVE LLPDITHEQI CEAVTEAFFR HYGERVDAEI ISPDKTPDLP NFAETFARQS
     SWEWNFGQAP AFSHLLDERF TWGGVELHFD VEKGVITRTQ VFTDSLNPAP LEALAEHLQG
     CQYRADVLQQ TCEALVAEFP EQESELRELA NWVAGAVR
//
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