ID Q7SBL5_NEUCR Unreviewed; 2275 AA.
AC Q7SBL5;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 144.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:EAA33781.1};
GN ORFNames=NCU08535 {ECO:0000313|EMBL:EAA33781.1};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA33781.1, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:EAA33781.1, ECO:0000313|Proteomes:UP000001805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC {ECO:0000313|Proteomes:UP000001805};
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA Lander E.S., Nusbaum C., Birren B.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002238; EAA33781.1; -; Genomic_DNA.
DR RefSeq; XP_963017.1; XM_957924.3.
DR SMR; Q7SBL5; -.
DR STRING; 367110.Q7SBL5; -.
DR PaxDb; 5141-EFNCRP00000004781; -.
DR EnsemblFungi; EAA33781; EAA33781; NCU08535.
DR GeneID; 3879184; -.
DR KEGG; ncr:NCU08535; -.
DR VEuPathDB; FungiDB:NCU08535; -.
DR HOGENOM; CLU_000395_5_0_1; -.
DR InParanoid; Q7SBL5; -.
DR OMA; PTPKGHC; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IBA:GO_Central.
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; IBA:GO_Central.
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:UP000001805}.
FT DOMAIN 51..559
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 203..400
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 686..760
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1507..1845
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1849..2164
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2275 AA; 254563 MW; B6A8B175C023D5BD CRC64;
MADTTASDAV VQASYAAKHN LAPHFIGGNR LENAPPSKVK DFVASHDGHT VITNVLIANN
GIAAVKEIRS VRKWAYETFG DERAIKFTVM ATPEDLQANA DYIRMADHYV EVPGGTNNHN
YANVELIVDI AERMDVHAVW AGWGHASENP KLPESLAASP KKIVFIGPPG SAMRSLGDKI
SSTIVAQHAD VPCIPWSGTG VSEVKVDDNG IVTVPDDVYL KGCVSSWQEG LEKAREIGFP
VMIKASEGGG GKGIRKVLNE DNFESLYNAA ASEIPGSPIF IMKLADSARH LEVQLLADQY
GNNISLFGRD CSVQRRHQKI IEEAPVTIAK PMTFKAMEEA AVRLGRLVGY VSAGTVEYLY
SHADDKFYFL ELNPRLQVEH PTTEMVSGVN LPAAQLQVAM GIPLHRIRDI RLLYGVDPRT
ASEIDFEFKN PESEKTQRRP TPKGHTTACR ITSEDPGEGF KPSNGVLHDL NFRSSSNVWG
YFSVGSAGGI HSFSDSQFGH IFAYGENRAA SRKHMVVALK ELSIRGDFRT TVEYLIKLLE
TEAFEENTIT TGWLDELISK KLTAERPDPI LAVVCGAVTK AHIASEGCMT EYRAGLEKGQ
VPSKDILKTV FPVDFIYEGY RYKFTVTRSS ADSYHLFING SKCTVGVRAL SDGGLLILLN
GRSHNVYWKE EVAATRMSVD SKTCLLEQEN DPTQLRTPSP GKLVKYTVEN GEHVSAGQTF
AEVEVMKMYM PLIAQEDGIV QLIKQPGATL EAGDILGILA LDDPSRVKQA QPFLGQLPEF
GAPVVVGSKP AQRFRLLYDT LQNILMGYDN QIIMQQTLKD LIEVLRDPKL PYSEFTAQFS
ALHARMPQKL DAQLTQVLEK ASSRSAEFPA RNLGKVFQKF LDENVASKVD AELLKTTLAP
LTTVIDQYSE GQKVHELNVI RDLLTSYVEV ERLFSGRRLQ DEEVILKLRD ENKEDIKKVT
QTVLSHSRVA AKNSLILAIL DEYRPNKPNV GNVSKYLRPV LRKLAELESR QTAKVSLKAR
EILIQCALPS LEERTAQMEH ILRSSVVESR YGETGWDHRE PSLDIIKEVV DSKYTVFDVL
TLFFAHEDPW VSLAALEVYV RRAYRAYVLK KIEYHTDETE TPSFLSWDFS LRKLGHSEFG
LPIQSAAPST PGTPVDSTFK RISSISDMSY LSHKTQDEPT RKGVIIPCKF LDDADELLSR
ALEKLPVLGA RKRNSVIPDL NEKRRPPLQR LETFDELSAV VNVAVRDAEG RSDEEILKEI
LPLVHQHRED LFARRVRRIT FVCGRNDGSY PGYFTFRGPE YVEDDSIRHS EPALAFQLEL
GRLSKFKIKP VFTENKNIHV YEAIGKGVET DKRYFTRAVI RPGRLRDEIP TAEYLISEAD
RVINDIFDAL EIIGNNNSDL NHMFLNFTPV FQLQPEEVEH SLQGFLDRFG PRGWRLRVAQ
VEIRIICTDP ATGMPYPLRV IITNTSGYVI QVELYAERKS EKGEWVFHSI GGTTKIGSMH
LLPVNTPYPT KNWLQPKRYK AHLMGTQYVY DFPELFRQAI QNSWVKAVRM DSSLADKQPP
VGECIEFSEL VLDDHDNLIE VSREPGTNTC GMVGWLIRAR TPEYPNGRKF VVVANDITFN
IGSFGPKEDN FFFKCTELAR KLGIPRIYLS ANSGARLGLA TELMPHFSVA WNDPSKPEAG
FKYLYLDDAG KKRFENTVIT EEITEGDEKR HKIVTIVGAE DGLGVECLRG SGLIAGATSR
AYNDIFTCTL VTCRSVGIGA YLVRLGQRAV QIEGQPIILT GAPALNNVLG RQVYTSNLQL
GGTQIMYRNG VSHLTANDDF AGVSKIVEWM SFVPDKRNNP VPISVSVDTW DRDVVYTPPQ
KQPYDVRWMI GGKEDENGYQ PGLFDKDSFV ETLGGWARTV VVGRARLGGI PMGVIAVETR
SVENITPADP ANPDSIEQVA NEAGGVWYPN SAFKTAQAIN DFNNGEQLPL MILANWRGFS
GGQRDMYNEV LKYGSFIVDA LVKFEQPVFI YIPPFGELRG GSWVVVDPTI NPVAMEMYAD
VDARGGVLEP EGIIGIKYRK DKQLETMARL DPVYADLKRQ SADASLPKEE SDAIKQKMTE
REQQLLPVYA QISVQFADLH DRAGRMKAKG VIREVLEWQN ARRFFYWRVR RRLNEEYILR
RIISATTPGG APSKALTASS TKERARHLQL LQAWSGIEKF DTADREVAVW YEENRHLVQT
KIDALKAEAI TTEMRDLIRA ASKGSDDAAW KGVRDILSVM PVEEREKVVK YLTTL
//
