ID A0A1A5XRY2_9BACL Unreviewed; 280 AA.
AC A0A1A5XRY2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Octanoyl-[GcvH]:protein N-octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_02119};
DE EC=2.3.1.204 {ECO:0000256|HAMAP-Rule:MF_02119};
DE AltName: Full=Octanoyl-[GcvH]:E2 amidotransferase {ECO:0000256|HAMAP-Rule:MF_02119};
GN Name=lipL {ECO:0000256|HAMAP-Rule:MF_02119};
GN ORFNames=A6764_03680 {ECO:0000313|EMBL:OBR56176.1}, A6764_11250
GN {ECO:0000313|EMBL:UYZ11450.1};
OS Brevibacillus sp. WF146.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=319501 {ECO:0000313|EMBL:OBR56176.1};
RN [1] {ECO:0000313|EMBL:OBR56176.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF146 {ECO:0000313|EMBL:OBR56176.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:UYZ11450.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WF146 {ECO:0000313|EMBL:UYZ11450.1};
RA Tang B., Tang X.-F., Zhu F., Li Y.;
RT "Complete genome sequence of Brevibacillus thermoruber WF146.";
RL Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the amidotransfer (transamidation) of the octanoyl
CC moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of
CC lipoate-dependent enzymes. {ECO:0000256|HAMAP-Rule:MF_02119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[lipoyl-carrier protein] + N(6)-octanoyl-L-lysyl-
CC [glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage
CC complex H protein] + N(6)-octanoyl-L-lysyl-[lipoyl-carrier protein];
CC Xref=Rhea:RHEA:20213, Rhea:RHEA-COMP:10500, Rhea:RHEA-COMP:10501,
CC Rhea:RHEA-COMP:10503, Rhea:RHEA-COMP:10504, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:78809; EC=2.3.1.204; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02119};
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]. {ECO:0000256|HAMAP-Rule:MF_02119}.
CC -!- MISCELLANEOUS: The reaction proceeds via a thioester-linked acyl-enzyme
CC intermediate. {ECO:0000256|HAMAP-Rule:MF_02119}.
CC -!- SIMILARITY: Belongs to the octanoyltransferase LipL family.
CC {ECO:0000256|HAMAP-Rule:MF_02119}.
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DR EMBL; LXGJ01000057; OBR56176.1; -; Genomic_DNA.
DR EMBL; CP109943; UYZ11450.1; -; Genomic_DNA.
DR RefSeq; WP_029099044.1; NZ_LXGJ01000057.1.
DR AlphaFoldDB; A0A1A5XRY2; -.
DR Proteomes; UP000093585; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016415; F:octanoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009107; P:lipoate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16443; LplA; 1.
DR HAMAP; MF_02119; LipL; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR024897; LipL.
DR PANTHER; PTHR43679:SF3; OCTANOYL-[GCVH]:PROTEIN N-OCTANOYLTRANSFERASE; 1.
DR PANTHER; PTHR43679; OCTANOYLTRANSFERASE LIPM-RELATED; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_02119};
KW Ligase {ECO:0000313|EMBL:UYZ11450.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000093585};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02119, ECO:0000313|EMBL:OBR56176.1}.
FT DOMAIN 38..240
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT ACT_SITE 140
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02119"
FT SITE 152
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02119"
SQ SEQUENCE 280 AA; 31264 MW; 12D3045A4DF7B062 CRC64;
MTFSVTQPFR WMDSGVYRDS PLEPLIRDEA LAAGMNREDA QPVIHLWVYD KALYLGRRDA
KLPRLEQALR RFGQEGFGCV LRSSGGACVP LDAGVLNLAC LLPDTSIAID AFFRFVAQML
HVGLREYGDM QFGEVTGSYC AGEYDFSIRG KKIGGMAQRR TRFGSILQLC INVEEQPRGA
WMERFYAEAG LVDMDKHRPI PFIDGSTVGS IAGLTGRAVT VPDVKERLLA AIRREWPISP
APFAVPESLM DESQHHLAER LGLFAFTADE LIRPDWRLPG
//
