GenomeNet

Database: UniProt
Entry: H2YHG1_CIOSA
LinkDB: H2YHG1_CIOSA
Original site: H2YHG1_CIOSA 
ID   H2YHG1_CIOSA            Unreviewed;       135 AA.
AC   H2YHG1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=lipoyl(octanoyl) transferase {ECO:0000256|ARBA:ARBA00012334};
DE            EC=2.3.1.181 {ECO:0000256|ARBA:ARBA00012334};
DE   AltName: Full=Lipoate-protein ligase B {ECO:0000256|ARBA:ARBA00030797};
DE   AltName: Full=Lipoyl/octanoyl transferase {ECO:0000256|ARBA:ARBA00033331};
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000256|ARBA:ARBA00031131};
OS   Ciona savignyi (Pacific transparent sea squirt).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000004760.1, ECO:0000313|Proteomes:UP000007875};
RN   [1] {ECO:0000313|Proteomes:UP000007875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA   Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA   Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA   Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA   Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA   Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA   Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA   Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA   Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA   Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA   Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA   Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA   Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA   Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA   Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA   Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA   Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA   Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA   Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA   Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA   Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA   Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA   Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA   Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA   Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA   Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA   Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA   Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA   Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA   Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA   Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA   Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA   Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA   Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA   Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAVP00000004760.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein]: step 1/2. {ECO:0000256|ARBA:ARBA00004821}.
CC   -!- SIMILARITY: Belongs to the LipB family.
CC       {ECO:0000256|ARBA:ARBA00007907}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; H2YHG1; -.
DR   Ensembl; ENSCSAVT00000004828.1; ENSCSAVP00000004760.1; ENSCSAVG00000002840.1.
DR   GeneTree; ENSGT00390000006450; -.
DR   HOGENOM; CLU_035168_3_1_1; -.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000007875; Unassembled WGS sequence.
DR   GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   CDD; cd16444; LipB; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR000544; Octanoyltransferase.
DR   InterPro; IPR020605; Octanoyltransferase_CS.
DR   NCBIfam; TIGR00214; lipB; 1.
DR   PANTHER; PTHR10993:SF7; LIPOYLTRANSFERASE 2, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR10993; OCTANOYLTRANSFERASE; 1.
DR   PIRSF; PIRSF016262; LPLase; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR   PROSITE; PS01313; LIPB; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007875};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..135
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
FT   ACT_SITE        134
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016262-1"
FT   BINDING         37..44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT   BINDING         103..105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT   BINDING         116..118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT   SITE            100
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016262-3"
SQ   SEQUENCE   135 AA;  15137 MW;  907754F3CD4D6CBA CRC64;
     MLQHDPVYTV GLRSSVYTEQ EESNLLAIGA DFVRTNRGGL ITFHGPGQLV VYPIFNLGAM
     KLGVREYVYQ LEETIINLCE RYKLHGERSP HTGVWIANDK ICAMGINTQR GITSHGLALN
     CNTDLKWFDR IVPCG
//
DBGET integrated database retrieval system