ID E4X484_OIKDI Unreviewed; 1943 AA.
AC E4X484;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBY23873.1};
GN ORFNames=GSOID_T00001202001 {ECO:0000313|EMBL:CBY23873.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY23873.1};
RN [1] {ECO:0000313|EMBL:CBY23873.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000861};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001455};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.
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DR EMBL; FN653024; CBY23873.1; -; Genomic_DNA.
DR InParanoid; E4X484; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001307; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.460.10; Biotin dependent carboxylase carboxyltransferase; 1.
DR InterPro; IPR049076; ACCA.
DR InterPro; IPR049074; ACCA_BT.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR013537; AcCoA_COase_cen.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR45728:SF3; ACETYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR Pfam; PF08326; ACC_central; 1.
DR Pfam; PF21385; ACCA_BT; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000001307}.
FT DOMAIN 1..251
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 379..453
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1196..1523
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1528..1838
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1943 AA; 219331 MW; 40244CA853AB4BCC CRC64;
MEFADSARHL EVQLLCDQLG NAISLYGRDC SIQRRHQKII EEAPQTIAPK DQWKNMEEGA
VRLAKLVGYH STGTVEYLYD PNKKRFCFLE LNPRLQVEHP CTEMISDVNL PATQLCVGLG
ISLDEMPLLT QEKPRGHVIA CRITAENPDE GFRPGSGTVQ ELNFRSSKNV WGYFSVVASG
ALHEYCDSQF GHIFAWGETR AQATSNLGMV LREISIRGDF RTTVEYLSHL IESETFRNSS
FSTGWLDFLI ASRDRPDAHD ERVSAICTAL HIADRHWTTV TQQYKSALEK GQILPLQSLP
PKELPLNLIL GNQLISLKIA RPASSSFCIE LNNTQLTLHI FRLSDSGILV QLNGVSYCAY
LQETAENLRV TINNQTVVFD KEKDPSLITS SSAGKLVRYL VEDGAPVVEG QDVAELEVMK
MVMTVKSALP GKIIHSKKPG AFLINGSVIA RLELGANLQV PKPEIYTRDF TDIHSSPSRD
MKNPPHRQLE KVIGNIHAVL DGFAVSGERV EKWVKRLVTS MFAIFRNRRL PLYEMREVMT
RLSGRIPAEL EGLINEDLKK YGTRLGSMLI RFPAMKILKH LNSYAGKLAT QEERTLHYVS
VSQIHSLCQK YADDIRGLQK NVVKEMLLKF TEVEKHFQSR TFEKSVKEIL IKNEDINKTT
EMILSHRNRI EKSKLIDEIL NVLLKHDGEM ILEMQNEIEG VACLRSFSCA LTARQVLITG
HQPSFQRRHN QIETIFLSAI DNSANALVFP DRLQQLVVSE TAIFDVLPEF FYHKLELVRF
AALEVYVQRA YTAYIIECVD TIPIGTSKAA VEFQFSLPCN HPSRQSSFGN IPTPGIAQNR
ESFPDLCIAG YEYEKNFEEL SRFGRTGLMV AYDNLEDFEN NIYDVLTCFG YLKSEDSDDD
ESDSSDLNAH PYMSDDDDPY AVHTLNVFLR SKKGGEDDEM LEKRFREFSQ VYQKDFRAAC
IRRITFAVHK KSHMPKFFTF RSRDEYREDE IYRHLEPALA FQLELSRLRN FTLKLYQTQN
HRMHLYHGIA KNKGGKEPID HRFFVRAIIR HSDLITEEAS FSYLRSEGER LLIESLDELE
VAIKSHSYKT DQNHVFLNFA PSVNMEANEV LNSVSEAVLK YGRRLWELRV TQAELKINVR
QDEETTSYRI FLSSEDGYRL ESHLYREVVQ SQKTIFLSIG PDEDPGPLNG LSTDTPYSTK
DLLQTARYKA QSAGCAYAYD YPSFFKSALK SSWEDKKVKH PKDFFTCNEL ILDKSGKLHE
VTRDPAQNTI GMVAWRMKFN QLTIQGKREI IVIANDSTVQ QGSFGPAEDD LFAAASKLAR
DEGIPRIYIT GNNSGARIGL SKDVQSCFQV AWKDQEAGLV EYFYLSSADY SKYSSQVIAE
HVTCESESRY KINAIIGSSD CGTAALKGSG LIAGETSKAY REIPTISLVT GRAVGIGAYL
VRLGQRVVQV ESSFVILTGF VALNSVLGSS VYSSNQQLGG PQIMSKNGVS HLTVADDYAG
IRTVIHWLSY IPVKGGLLDI PKIICDDPPE RQVTVEIKEK TYEARRILAG DSEHLGILDR
GSLLELQPDW AKTVLIGRGR LGGIPIGIIA AETRQVTSLV PADPADRNSQ EKIITQAGSV
WFPDSAFKTA QAIRDIDQEG LPLLILANWR GFSGGMKDMY DQVLKFGAMI VDALSEYKSG
PVLVYIPPLG ELRGGAWAVL DKSINPAKIE LYADPNSRSG VLEPEGTVKI KMKEKNLQEL
MCRFDSQMKE LQTTLNSGSL TTEQIGTTSE LSHLRSKSLQ DAYHNLAIQF ADLHDMPQAV
ANKQCLTKVV PLAECRKFLY NRLRRKLLED KCVDLIKDSD PDVTRDEAIA TLERYFFQNH
LKSGVKWEED VPVEKWLAEQ IENANSHLNI MIQQNQSDIM LKQVLKLSEN QEVDQIADVV
QSLLDSLSDE KQKQVLSIIN VNR
//
