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A8I2V9

- LISC_CHLRE

UniProt

A8I2V9 - LISC_CHLRE

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Protein

Lipoyl synthase, chloroplastic

Gene

LIP1P

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.UniRule annotation

Catalytic activityi

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.UniRule annotation

Cofactori

Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi155 – 1551Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi160 – 1601Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi166 – 1661Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi183 – 1831Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi187 – 1871Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi190 – 1901Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase, chloroplasticUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthaseUniRule annotation
Short name:
LSUniRule annotation
Short name:
Lip-synUniRule annotation
Lipoate synthase, plastidialUniRule annotation
Short name:
LIP1pUniRule annotation
Lipoic acid synthaseUniRule annotation
Gene namesi
Name:LIP1PUniRule annotation
ORF Names:CHLREDRAFT_196092
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas
ProteomesiUP000006906: Unassembled WGS sequence

Subcellular locationi

Plastidchloroplast UniRule annotation

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040ChloroplastUniRule annotationAdd
BLAST
Chaini41 – 430390Lipoyl synthase, chloroplasticPRO_0000398859Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi3055.JGI196092.

Structurei

3D structure databases

ProteinModelPortaliA8I2V9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
InParanoidiA8I2V9.
KOiK03644.
OMAiRKVDCDI.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
MF_03129. Lipoyl_synth_plantC.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027526. Lipoyl_synth_chlpt.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A8I2V9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRSLATLHQS PASCSRSAPV APCPARRANS SRRVARQGPR ARASSPVVET
60 70 80 90 100
ESEDVDITPQ IDAFEELVRL AVEKDPSLAT LAEQHLRSKS KSAAPVSPFA
110 120 130 140 150
APSPGSPSAS SMLGPSLGAL PNQNKPAWLR QRAPQGEIYS GLKDQLRGLK
160 170 180 190 200
LATVCEEAQC PNIGECWNGE LATATIMLLG DTCTRGCRFC AVNTARTPPP
210 220 230 240 250
PDPNEPVNTA TAVASWGVGY VVLTSVDRDD MPDGGSEHFA ATVRTLKQLR
260 270 280 290 300
PGILVECLTP DFKGDLDAVR HLARSGLDVY AHNVETVERL QKRVRDPRAG
310 320 330 340 350
YMQTLDVLRA AKECGVYTKS SIMLGLGETD DEVIDTMLDL KAVGVDIFTL
360 370 380 390 400
GQYLQPTPHH LPVTEFVTPE KFEYWRKFGQ EEIGFRYVAS GPMVRSSYKA
410 420 430
GEFFLHSMIE SDRAKARAAQ EGAAGRVRPL
Length:430
Mass (Da):46,680
Last modified:December 4, 2007 - v1
Checksum:i8C549FCC6E98116E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS496112 Genomic DNA. Translation: EDP07358.1.
RefSeqiXP_001699662.1. XM_001699610.1.

Genome annotation databases

EnsemblPlantsiEDP07358; EDP07358; CHLREDRAFT_196092.
GeneIDi5725443.
KEGGicre:CHLREDRAFT_196092.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS496112 Genomic DNA. Translation: EDP07358.1 .
RefSeqi XP_001699662.1. XM_001699610.1.

3D structure databases

ProteinModelPortali A8I2V9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3055.JGI196092.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi EDP07358 ; EDP07358 ; CHLREDRAFT_196092 .
GeneIDi 5725443.
KEGGi cre:CHLREDRAFT_196092.

Phylogenomic databases

eggNOGi COG0320.
InParanoidi A8I2V9.
KOi K03644.
OMAi RKVDCDI.

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00206. Lipoyl_synth.
MF_03129. Lipoyl_synth_plantC.
InterProi IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027526. Lipoyl_synth_chlpt.
IPR007197. rSAM.
[Graphical view ]
PANTHERi PTHR10949. PTHR10949. 1 hit.
Pfami PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF005963. Lipoyl_synth. 1 hit.
SMARTi SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00510. lipA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The Chlamydomonas genome reveals the evolution of key animal and plant functions."
    Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J., Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L., Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H., Kapitonov V.V., Ren Q., Ferris P.
    , Lindquist E., Shapiro H., Lucas S.M., Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L., Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H., Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M., Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C., Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J., Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C., Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J., Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P., Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R., Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P., Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y., Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L., Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.
    Science 318:245-250(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CC-503 and cw92.

Entry informationi

Entry nameiLISC_CHLRE
AccessioniPrimary (citable) accession number: A8I2V9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 4, 2007
Last modified: October 29, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3