ID W4I806_PLAFA Unreviewed; 3368 AA.
AC W4I806;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETW39537.1};
GN ORFNames=PFNF135_05567 {ECO:0000313|EMBL:ETW39537.1};
OS Plasmodium falciparum NF135/5.C10.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=1036726 {ECO:0000313|EMBL:ETW39537.1, ECO:0000313|Proteomes:UP000019114};
RN [1] {ECO:0000313|EMBL:ETW39537.1, ECO:0000313|Proteomes:UP000019114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF135/5.C10 {ECO:0000313|EMBL:ETW39537.1,
RC ECO:0000313|Proteomes:UP000019114};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Annotation of Plasmodium falciparum NF135/5.C10.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETW39537.1, ECO:0000313|Proteomes:UP000019114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF135/5.C10 {ECO:0000313|EMBL:ETW39537.1,
RC ECO:0000313|Proteomes:UP000019114};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum NF135/5.C10.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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; KI926126; ETW39537.1; -; Genomic_DNA.
DR EnsemblProtists; ETW39537; ETW39537; PFNF135_05567.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000019114; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 2.40.460.10; Biotin dependent carboxylase carboxyltransferase; 1.
DR Gene3D; 3.90.1770.10; PreATP-grasp domain; 1.
DR InterPro; IPR049076; ACCA.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
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; IPR016185; PreATP-grasp_dom_sf.
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; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 2.
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; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..3368
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004842624"
FT DOMAIN 500..1147
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 652..844
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1301..1375
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 2601..2858
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 2971..3290
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 110..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1768..1795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2408..2427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3281..3308
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 3368 AA; 395151 MW; 0508A37AB1CC45DA CRC64;
MINFFLSLLL FVLFFENLVV SIKYRNIHYI HMPNNAHNKN FNEKENREIY HNVNISGGNT
IYEEPKNKYI TLFLSNGKKI LHSIFRNNNN NNITICNENT GKNSNINLKN NSENNTKNNS
KNYSRGSSSC LNIQNVSNTY YDKRRIKKDI MNKKVEENLI HDENENNIIN DKICCDEKQD
LDKEIHVDEQ NEKKSNSTLN NESFISILSN DNSEKKKDME ESNNYSNNFY LNSLEENIIY
PTQHVDCDFN GKWKSHVDDI LENDSYYSNM NDNSNKSCIS DYELLKTSIL LNNTKDDFPL
YENSRKNILT TSGKINKNKN LKERKKKNLN RLFYTLKLTN NFSFKNSKNR RKYTNSYNSG
SSTHSRYVMD NKEYIIYHNN NNNNNNNNYN SYSNNCNNMY IQGNKKKYNR LYCKKSANSQ
EKDYDKDINL IASYKINSEL SQDDLKYNSQ IINMPNDHFN IITSDEKENI KKNAYKNYVN
YINERRYGYF DLLEKKNEKI IRKLLIANNG MAALKCILSL KDWLFKKFYD ENLIKIIVMA
TDEDIKSNAK YISLADKVIK VPGGKNIHNY ANVPLIVELA KSENVDAVWP GWGHSSENPL
LSTLLEKENI IFIGPTGNVM EALGDKISAN ILAQSVEVPV VKWSGDNIRI DKFENNKIND
ELYNNATIHS LDDCIKECKR IGFPVMIKAS QGGGGKGIRK VENEYEIKKA YEQVQNELPN
SPIFLMKVCN NVRHIEIQVV GDMYGNVCSL SGRDCTTQRR FQKIFEEGPP SVVPYPIFRE
MEKSSIRLTK MIKYRGAGTI EYLYDQINKK YFFLELNPRL QVEHPVSEGI TNCNLISIQL
QVAMGIPLQN IDDIRNLYQI DKIEKIKKKD EQKKEFELTD NLCNDTINKD NINNDNIYKD
NINNDNINND NIYKDNIYKD NINNDNIYKD NIYKDNIDND NIYKDNIYKD NIYNDNIYKD
NINNDNIHHI DNTTNEQNNK NLLHYNNYRN QNLCNNNSIK SLLNYDTNEN VNRKYNLLNE
HFDFYNNKPY IKNHVIAARI TAENSNDSFK PTSGNVRRIN FQNWKDVWGY FSINDGFVHE
FSDSQIGHIF AKGETREVAR KNLILALRKL HIDGDIKTGT KYLAKILESK AFIDNNITTN
WLDIIIEKKK HVFYNTCHII LLCATIFKLL IYFMNEKGKV EENLDRDDIA IKRDKNYGNV
INKNNNHSGN INNNGEHMCK MKSAYIFDMI FQNIKYPFKG YNIGENLYQL EINGQEIEIS
AEYDKNNNKV FSTFNNQTYI YACSEDTLGI HMQLEKDNIF IPNVRNPYHL ISNTNGKIVK
YLINDGEEVK KNDDYIEVEA MKMIMTFKST ESGILRHKLS EGTIIKIGDL LGIIEKKDND
KKHIKQDNEI QYFNGHLDLS NKYTYELIDN RTIFPNILDD NYNKSCDNSY AFTDNMSLQN
SEEHYLVKDE QKKKKKKNIS SILNNNMVSI KTVSNDLTDN INVLRAETLS EEGLKDEMYH
GQMCDDRMCD DQMCDDENVV KKNDKEQNKS HKNLKENNMD ECTYEDDNYI YMKENQKKKL
FMKQNRKKIF RLFSNDNEKI TTALNYLNDK FHCVKNYLSN LNFSSANSVS DSSNSSYQNN
KNNNNNNDNN NNNYNNNNNN NNNSKNKKKN NSVQYNYSNA KYSNVNMIHK YDKKPFDKSY
LMNEVNSNNV NVLKMKNKNN STFPLIENLE NNISTEIMSS RNTSNEKILH NNISKDNTIS
EPIFNNNSSD ESNINNITFF NNLSNNGSIR KRNNNNNSSS SNNNNNNNNK NNNFKHSYYM
DYNNDNIYWN HVKNEKSKYL LDIPIMKRIE FLLKGYEQDY EKCFDELINK KDIKNVSNWS
AYIINNINDI LDTFIQYNIL FSKKEFISEI DLYDILYNNI RDKKKQYEII HAYTYNDLSI
KFIEKILKYI LNNINSNLAF DIILDKLKIL AEFKGKIFRN IIVLSRHILF LLEGLELIEY
IKIALNYNDN KNMKNGGKLS NNMLLLSNYM KKNNLDFSKM IEYKNNKNDI EIVNMFFKGH
SSNIHMFVPS LIKSNKNSMF LKFYLNNLYK YCNIKSIMVT NNIIKFSINN SEYTNLLIWN
ENDTIDINKI LLSDIKINND RYLNTVHIIN TNNELCLHPS HSFEENIIKN KILQKCKKLY
IYNYANNKYG DIYEWKNEDL SKGLVGKYSK DGSINNILPY EEYIFGNEKE ILEYYELKNI
NQAIYEKTKI FFGIYKNNKN DNNIRNNVNN NYTSLFGHRV IDFNDIKNTT NEYNNFEEHN
YQDDKFIFNK DIHNILLELK ESLNDISRGR LNTLIRDNKI SSYIIYHIIV DDMMDIETIK
EAYKVFMIKY NEMILENYVN NIFIKIYRTN KKSCTENAPQ IQLERMFKLN VLLNKGGVKK
ERTDRYNVED DNNKKDNDNK YNCNNNNNDD NKYDCNNNFY YDNKYDCNNN FYHDNKFNCN
NNYYHNYHFV EEINQFPSFQ IDTLYMKRKR AREVDTLYAY DFINLINISL NRSNKNRESH
KICNYINSIK EFKLKSDMIC YNSNSDNLKN HAMNIKSAHI PLEKKEEYLF EHFDNLSNYE
IKIRKSLYLS DKLDIGQNKR SVVGLLLNIR TDEYEEGRDV IFIINDISTQ GGSFSIFEDE
LFYGISSYAR EKKIPRIYIS CNSGARIGLY NFLMDKIRIE WKDEQKKELG YKYIYITQDV
KEQIDKEDII FLTEIIENNE KRYIIDAIVG NLKNPVGVEN LRGSGLIAGE TSKAYEEIFT
LSYVTGRSVG IGAYLVRLGK RTIQKKGSSL LLTGFNALNK ILGENVYVSN EQLGGVNIMM
RNGISQVQVE SDQEGMDKII QWLSYVPRTS NDYYDLIQNI YKENNRKFLQ NNNFLITNKQ
KTMNTYNNLF IHNNKNVSNS VDIKDNIKNQ IDTNINTETN INVQDLNIIK KNGINTKSKQ
DENVYEKKDK VEEIYKDQNT YSTNNSKTSK PNDNSMSSYN FELLHINDMD YDHIDDSNII
DLIKGTQEEQ GFLDKNTYFE YMNEWGKGII TGRGKLGSIP VGFIAVNKNL VTQSIPCDPA
LKTKAQKLIQ APCVFFPDNS FKTAESIEDF NKENLPLFIF ANWRGFSGGS MDMFYGILKF
GSMIVNQLVN YKHPVFVYIP ISAELRGGSW VVVDETLNSQ IIEMYADVNS KGGILEPPGI
VEVKFRYPDI RKLMHSIDTT IIALNEKMAR CENDEEKNNI KKDIEIKEKE LLPYYLQVCH
KYADLHDMSA CMKAKGVIRK IVPWNKARSF FYYRLMRRLL INILSRKYDN ALIKNEEIEN
ILNDLNNSED DDYIVCNRVF NNNILRNLKY DTKDIIYNKT LNDFLKIFKM LSQEQRTEFL
NKINSYEN
//
