ID A0A2B4S0A4_STYPI Unreviewed; 1146 AA.
AC A0A2B4S0A4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000313|EMBL:PFX22463.1};
GN Name=leuC {ECO:0000313|EMBL:PFX22463.1};
GN ORFNames=AWC38_SpisGene13007 {ECO:0000313|EMBL:PFX22463.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX22463.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX22463.1}.
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DR EMBL; LSMT01000239; PFX22463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4S0A4; -.
DR STRING; 50429.A0A2B4S0A4; -.
DR EnsemblMetazoa; XM_022939904.1; XP_022795639.1; LOC111334209.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR002898; MotA_ExbB_proton_chnl.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF01618; MotA_ExbB; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 468..490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 567..591
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 611..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 679..697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..155
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 103..1146
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 222..423
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 1146 AA; 123749 MW; 3B122B615F1EC86D CRC64;
MKIKDIQNFI KFVSKSGVAQ VTLEVDNVKI SIKNELKKSE FVAPQQPTII TSNTPTPSIS
ASGEEVSKTA VEEAPNPKYK EITSPMVGTF YRKANPKKPN LVEVGSSVTA DTDVCVLEAM
KTFNEVKAGI NGKIVEILVE DASPVEFEEA VCIGPAVSSE SYLDVVKILA AAEITNADAI
HPGYGFLSEN AHFSELCATH NIKFIGASAE MINRMGDKAA AKATMIAAGI PTVPGSEGIL
DSFEEAEKLA KEVGYPVMLK ATAGGGGKGM RAVWKASDLL DAWESARQES KAAFGNDDMY
LEKLIEEPRH IEIQIMGDSK GRACHFSERD CSVQRRHQKL TEEVPSPFMT KVLREKMGAS
AIKAAEFIKY EGAGTVEFLV DKHRNFYFME MNTRIQVEHP ITEEVVLLAQ EAQTEETTEQ
TAVSTDTTSV ENTGVVNDTE ATTEDEVEEA EQSFHQVLKQ RFIEGGPFFM GIVLVALILG
LAIAIERIIY LNLATTNTKK LIQEVEGALS SDGVDAAKEV CKNTNGPVAS IFYQGLDRIE
ESIESAEKSV IGYGGVQMGL LEKNISWLSL FISLAPMLGF MGTVIGMIGA FDSIQAAGDI
SPTVVAGGIK VALLTTVFGL VVAIILQIFY NYIVSKVDGI VNDMEDASIT LVDMLVNRVI
AKGDEVIITE QGAGIVGPFV YYAVALLIAT AGISYGVSDD SAVKDVIGQV IEGGEQGANS
KWVSTGTPNT VPTPIKARPT VAEVVQELPV KREMTIAIKT QAGLKNRGIG VMYPNRTFAT
ADHNTPTKNQ HLPVADPLSA NQLKALSENT KKHGISHWGL GHKKNGIVHV VGPENGITLP
GATIVCGDSH TSTHGAFGAI AFGIGTSEVE MVLATQCIMQ PKPKKMRITV DGTLAKGVTS
KDVALYIIAQ LSASGATGFF IEYAGSVFRE MSIEGRMTVC NMSIEMGARG GMVAPDAKTF
DYIKGRLHTP KGKAWKKAMQ YWQKLYTEED AVFDKEYQFS GAAITPMITY GTNPGMGISI
TKNIPKSEEV FEAKATYEKS LQYMNYKTGE AMQGKAIDYV FVGSCTNGRV EDFRAFASVI
KGRKKAANVT VWLVPGSHLV VDVLQKEGII DTLKEAAGIN VFIPPINLLY VVYDARSFCG
KCRDEQ
//
