LIPL_ALKHC
ID LIPL_ALKHC Reviewed; 278 AA.
AC Q9K6A7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Octanoyl-[GcvH]:protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_02119};
DE EC=2.3.1.204 {ECO:0000255|HAMAP-Rule:MF_02119};
DE AltName: Full=Octanoyl-[GcvH]:E2 amidotransferase {ECO:0000255|HAMAP-Rule:MF_02119};
GN Name=lipL {ECO:0000255|HAMAP-Rule:MF_02119}; OrderedLocusNames=BH3822;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 2-278.
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of a hypothetical protein from Bacillus halodurans:
RT Pfam-PF03099.";
RL Submitted (FEB-2009) to the PDB data bank.
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_02119}.
CC -!- MISCELLANEOUS: The reaction proceeds via a thioester-linked acyl-enzyme
CC intermediate. {ECO:0000255|HAMAP-Rule:MF_02119}.
CC -!- SIMILARITY: Belongs to the octanoyltransferase LipL family.
CC {ECO:0000255|HAMAP-Rule:MF_02119}.
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DR EMBL; BA000004; BAB07541.1; -; Genomic_DNA.
DR PIR; F84127; F84127.
DR RefSeq; WP_010899947.1; NC_002570.2.
DR PDB; 2P5I; X-ray; 2.21 A; A=2-278.
DR PDBsum; 2P5I; -.
DR AlphaFoldDB; Q9K6A7; -.
DR SMR; Q9K6A7; -.
DR STRING; 272558.10176447; -.
DR EnsemblBacteria; BAB07541; BAB07541; BAB07541.
DR KEGG; bha:BH3822; -.
DR eggNOG; COG0095; Bacteria.
DR HOGENOM; CLU_067270_0_0_9; -.
DR OMA; VQIYLCI; -.
DR OrthoDB; 871298at2; -.
DR EvolutionaryTrace; Q9K6A7; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0016415; F:octanoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009107; P:lipoate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 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 Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..278
FT /note="Octanoyl-[GcvH]:protein N-octanoyltransferase"
FT /id="PRO_0000410836"
FT DOMAIN 44..249
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 148
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02119"
FT SITE 160
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02119"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:2P5I"
FT HELIX 27..41
FT /evidence="ECO:0007829|PDB:2P5I"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2P5I"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:2P5I"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:2P5I"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:2P5I"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:2P5I"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:2P5I"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2P5I"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:2P5I"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:2P5I"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2P5I"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2P5I"
FT STRAND 159..169
FT /evidence="ECO:0007829|PDB:2P5I"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:2P5I"
FT HELIX 185..200
FT /evidence="ECO:0007829|PDB:2P5I"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2P5I"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:2P5I"
FT HELIX 230..243
FT /evidence="ECO:0007829|PDB:2P5I"
FT HELIX 255..275
FT /evidence="ECO:0007829|PDB:2P5I"
SQ SEQUENCE 278 AA; 31000 MW; 5858056515F4FFFA CRC64;
MSLLLQQHLS QPWRFLDHTS FGPTFQALQS FAYDDTLCTS IGKSQSPPTL RAWVHHNTVV
LGIQDSRLPQ IKAGIEALKG FQHDVIVRNS GGLAVVLDSG ILNLSLVLKE EKGFSIDDGY
ELMYELICSM FQDHREQIEA REIVGSYCPG SYDLSIDGKK FAGISQRRIR GGVAVQIYLC
VSGSGAERAK MIRTFYDKAV AGQPTKFVYP RIKPETMASL SELLGQPHNV SDVLLKALMT
LQQHGASLLT ESLSADEWLL YEQHFARISE RNEKLLAE
