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Database: UniProt
Entry: A0A367KTR3_RHIST
LinkDB: A0A367KTR3_RHIST
Original site: A0A367KTR3_RHIST 
ID   A0A367KTR3_RHIST        Unreviewed;      2216 AA.
AC   A0A367KTR3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Acetyl-coenzyme-A carboxylase {ECO:0000313|EMBL:RCI05537.1};
GN   Name=ACC1_2 {ECO:0000313|EMBL:RCI05537.1};
GN   ORFNames=CU098_003035 {ECO:0000313|EMBL:RCI05537.1};
OS   Rhizopus stolonifer (Rhizopus nigricans).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=4846 {ECO:0000313|EMBL:RCI05537.1, ECO:0000313|Proteomes:UP000253551};
RN   [1] {ECO:0000313|EMBL:RCI05537.1, ECO:0000313|Proteomes:UP000253551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSU 92-RS-03 {ECO:0000313|EMBL:RCI05537.1,
RC   ECO:0000313|Proteomes:UP000253551};
RX   PubMed=29674435; DOI=10.1534/g3.118.200235;
RA   Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA   Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA   Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA   Heitman J., Vilgalys R., Stajich J.E.;
RT   "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL   G3 (Bethesda) 8:2007-2018(2018).
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}.
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:RCI05537.1}.
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DR   EMBL; PJQM01000363; RCI05537.1; -; Genomic_DNA.
DR   STRING; 4846.A0A367KTR3; -.
DR   EnsemblFungi; RCI05537; RCI05537; CU098_003035.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000253551; 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:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion 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; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; IPR049074; ACCA_BT.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR013537; AcCoA_COase_cen.
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; 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; PF08326; ACC_central; 1.
DR   Pfam; PF21385; ACCA_BT; 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; 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; 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; 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; 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   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000253551}.
FT   DOMAIN          37..545
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          192..386
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          672..746
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1458..1797
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1801..2116
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   2216 AA;  248792 MW;  809A05EDF2614A7A CRC64;
     MVDHKSLPSH FLGGNSVETA TQSPVKEFVE AHEGHTVISK VLIANNGMAA MKEIRSVRKW
     AYETFGNERA IEFTVMATPE DLKANAEYIR MADNYVEVPG GTNNNNYANV ELIVDVAERT
     GVHAVWAGWG HASENPRLPE MLAKSKHKCL FIGPPASAMR SLGDKISSTI VAQHAQVPTM
     GWSGDNITDV VADASGHVTV PDEAYAKACV KTAEEGLAAA EKIGFPVMIK ASEGGGGKGI
     RMVKDSTNFT QLFAQVQGEI PGSPIFIMKL AGNARHLEVQ LLADQYGNAI SLFGRDCSVQ
     RRHQKIIEEA PVTIAKPDIF EQMEKAAVRL GKLVGYVSAG TVEYLYSHHD DQFYFLELNP
     RLQVEHPTTE MVSGVNLPAA QLQIAMGIPL HRIRDIRVLY GVEHNSASEI DFNFEHPTSL
     TSHRRPTPKG HVIACRITAE NPDAGFKPSS GIMQELNFRS STNVWGYFSV VSAGGLHEYA
     DSQFGHIFAY GENRQAARKN MVIALKELSI RGDFRTTVEY IIRLLETPDF EENTINTGWL
     DMLISKKLTA KRPDTMLAVF CGAATKAHAA ALECFQQYKQ SLEKGQVPSK GTLKTVFTVD
     FIYEEVRYNF TVTLSAPGLY TLYLNGSKTQ VGIRDLSDGG LLISIDGKSH TTYSRDEVQA
     TRLMIDGKTC LLEKESDPTQ LRSPSPGKLV NLLVENGDHL KAGDAYAEIE VMKMYMPLVA
     TEDGHVQFIK QAGATLEAGD IIGILSLDDP SRVKHALPFS GTVPAFGPPH IIGDKPAQRY
     NATKHTLEHI LQGYDNQALV QTVVKDFADI LNDPELPYSE LSAVLSVLSG RIPQRLEASI
     HKLFDESKAA QREFPAVEFL KLIEDFAREN VTLQSEATAL KNAVAPLVSI FERYRNGLKE
     HAYSNYVQLM EQYYDVEIMF SQQRDEEVIL SLRDQNKDNL DKVLEVVLSH AKVNIKNNLI
     LMLLEIINPV ATGNALDKYF TPILKRLSEI ESRGTQNVTL KARELLILCQ LPSYEERQAQ
     MYQILKSSVT ESVYGGGTEY RTPSYDAFKD LIDTKFNVFD VLPHFFYDAD PYIALAAIEV
     YCRRSYHAYK ILDVAYNLEH KPYVVAWKFL LQTAATSIDP NKRIASYSDL TFLLNKTEEE
     PVRTGAMTAC NSLEDLEAEL PRILTAFEEE PLPPMLQRNA PPKETRMENI LNIAIRADDT
     LDDAAFRTKI SDVIASHADA FRQAHLRRIS VVVCRDNQWP DYYTFREREN YQEDQTIRHI
     EPAMAYQLEL ARLSNFDIKP CFIENRQMHV YYAVAKENPS DCRFFIRALV RPGRVKSSMR
     TADYLISESD RLLTDILDTL EIVSHEYKNS DCNHLFINFI PTFAIEAEDV EHALKDFVDR
     HGKRLWKLRV TGAEIRFNVQ SKRPDAPIIP MRFTVDNVSG FILKVEVYQE VKTEKNGWVL
     KSVNKIPGAM HMQPLSTPYP TKEWLQPRRY KAHLMGTTYV YDFPELFRQA VQNQWNQAIK
     HDSSLKQPSH LVEAKELVLD EDDVLQKIDR APGTNTVGMV AWLMTIRTPE YPSGRRIIAI
     ANDITFKIGS FGVAEDQVFY KASELARSLG IPRVYLSANS GARIGLAEEL IGQFKAAWKN
     PADPTAGFNY LYLTPADYDA LVQQGDAKSV LVEEIQDEGE TRLRITDVIG HTDGLGVENL
     KGSGLIAGAT SRAYDDIFTI TLVTCRSVGI GAYLVRLGQR TVQNEGQPII LTGAPALNKV
     LGREVYTSNL QLGGTQIMYK NGVSHLTAEN DFEGIGKIIQ WLSFVPEVRN GPVTMRMGVD
     PVDRDIEYMP PKGPSDPRFF LAGKNDENGK WLSGFFDQDS FIETLSGWAR TVVVGRARLG
     GIPMGVVSVE TRTVENIVPA DPANSDSTEQ VFMEAGGVWF PNSAYKTAQA INDFNKGEQL
     PLMIFANWRG FSGGQRDMYN EVLKYGAKIV DALSNYKQPV FVYIIPNGEL RGGAWVVVDP
     TINKDMMEMY ADTHARGGVL EPEGIVEIKY RKPALLATME RLDETYASLK KQLAEEGKTE
     EEKATLKTQL EAREQELLPV YQQISIQFAD LHDRSGRMKA KGVIRKALDW RRARQYFYWR
     VRRRLCEEYT FRKITTATNS TMSREQMVTL VKQWFTNDNE SVDFDDADEI VAEWFDKRAS
     VIEQRITKIK SDSLKQQVTS LGAVDQEAVI EGFSELLENL SQDARAEILR KLNSRF
//
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