ID A0A197K7T6_9FUNG Unreviewed; 2226 AA.
AC A0A197K7T6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:OAQ33555.1};
GN ORFNames=K457DRAFT_133928 {ECO:0000313|EMBL:OAQ33555.1};
OS Linnemannia elongata AG-77.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ33555.1, ECO:0000313|Proteomes:UP000078512};
RN [1] {ECO:0000313|EMBL:OAQ33555.1, ECO:0000313|Proteomes:UP000078512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-77 {ECO:0000313|EMBL:OAQ33555.1,
RC ECO:0000313|Proteomes:UP000078512};
RG DOE Joint Genome Institute;
RA Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA Bonito G.;
RT "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT the earliest lineages of terrestrial Fungi.";
RL Submitted (MAY-2016) 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; KV442020; OAQ33555.1; -; Genomic_DNA.
DR STRING; 1314771.A0A197K7T6; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000078512; 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; 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; 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:UP000078512}.
FT DOMAIN 34..542
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 191..383
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 669..743
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1455..1797
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1801..2119
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2226 AA; 249342 MW; B2D0C7FE5CB868E6 CRC64;
MTSNVQSFIG GNALDKAPAG AVHDFVSQHG GHSVITKILI ANNGIAAVKE IRSVRKWAYE
TFGDERAIQF TVMATPEDLK VNAEYIRMAD QYVEVPGGSN NNNYANVDLI VDIAERTGVH
AVWAGWGHAS ENPKLPESLR DSPQKIIFIG PPGSAMRSLG DKISSTIVAQ SADVPTMGWS
GTGITETEMD PNGFVTVPED AYQAACVTDA EDGLKKAHAI GFPIMIKASE GGGGKGIRKV
EDPEKFAQAF HQVLGEVPGS PVFIMKLAGN ARHLEVQLLA DQYGHAISLF GRDCSVQRRH
QKIIEEAPVT IAKPDTFEAM EKAAVRLAKL VGYVSAGTVE YLYSHATDTY FFLELNPRLQ
VEHPTTEIVS GVNLPAAQLQ IAMGLPLNRI KDIRVLYGLQ PSGTSEIDFE FAQQVSFETQ
RKPAPKGHVI AVRITAENPD AGFKPSSGMM HDLNFRSSTN VWGYFSVSSA GGLHEFADSQ
FGHIFAYGQD RGQSRKNMVV ALKELSIRGD FRTTVEYLIR LLETQEFEEN TINTGWLDSL
ISNNLTAERP ETMLAVMCGA VNRAHTISEN CLKEYKKSLE KGQIPSKDVL RSVNQLDFIY
DGVRYNFTAT RSGPNSYTMY LNGSMISISV RPLTDGGLLV LLDGKAHTTY SLEEVQATRL
MVDGKTCLLE KENDPTQLRS PSPGKLVRFL VESGDHVKAS QAYAEIEVMK MYMPLIATED
GIVQFIKQPG TTLDAGDIIG ILSLDDPSRV KHAKPFEGQL PPMGQPTIHG AKPHQRYREL
RLILDNAMDG YDNQALVQPT LKEIFEVLQT PELPYLEFNE VFAALSGRIP PKLEISLHQE
VDQSMKNHEH FPARTLQALI DAHCRANFSK PADVSSFLAS VAPLTTIIQE YQTGLKTHSW
TFIAHYLTKY HEVESLFDDS AREEETILAI RDQYKDDVEK VINIALSHSR VTAKNNLVLS
LLDQIKPTSS GGALDKFFSP ILKKLAELNG RLTSKVSLKA RELLIHVQLP SFEERQAQME
KILRSSVTEE IYGGDHEARM PNYDNLKELV DTTYTVFDVL PNFFYHESAH VRLAAFEVYC
RRAYHAYEIL DINYHMEHNP LLITWKFLLN TPNKSSEGGP NRVASVSDMS YLINKADPEP
VRTGGILAVR DIKELEGRFQ SVLDFFPTVK SNKHLAHVQA TSVHNNVLNV VLKSESIHPN
DDDYWLNLLS PIVKGQSEHL RSHGIRRMTF LIFRQGNYPS YFTFRERNNY AEDQTIRHIE
PAMAYRLELS RLSNFDIKPC FIDNRQVHVY YAVGKENVSD CRFFVCALVR PGRLRSSVRT
ADYLISETDR LLNDILDALE IVGATYKQSD CNHLFINFIP TFQLDATEVE SALKGFIDRH
GKRLWRLRVT GAEIRFNVQS KNDAADPIPL RFIISNVSGY VLNVDTYREI QTDKGAIFKS
VGPSGPFHLL PVNQPYPTKE WLQPRRYKAH LMGTTYVYDF GELFRQAVRA QWNHAVKVNP
SLKAPNQVLE MRELVLDEKQ QLQQVVREAG SNNCGMVAWI FTLRTPEYPE GRQIIVIAND
ITYNIGSFGP EEDLVFYKAS ELARKLGIPR VYLSANSGAR IGLASEVIGL FNSCWNDASN
PSKGFKYIYL TDAGLKQLEA QEERSGKKSV LTETVVEDGE TRHKITDVIG AVDGLGVENL
RGSGLIAGET SRAYDDIFTI TLVTCRSVGI GAYLVRLGQR TIQNEGQPII LTGAPALNKL
LGRDVYTSNL QLGGTQIMYK NGVSHLTAQN DYEGIGKIVN WLSYIPERKN APVPITVSND
TWDRDIDYLP PKGAVYDPRW LIGGKDAEEE GAAFQTGFFD KGSFTETLTG WARTVVVGRA
RLGGVPMGVI AVETRSVEHI IPADPANGDS VEQVLMEAGN VWYPNSAYKT AQAINDFNKG
EQLPLMIFAN WRGFSGGQRD MYNEILKYGS FIVDALSSYK QPVFVYVVPN GELRGGAWVV
VDPTINENMM EMYADKRSRA GVLEPEGIVE IKFRKAQLLA TMERLDDKYR DLKAQYEKPD
LAGADREAIK TKLTEREQEL LPVYQQLAIQ FADLHDTAGR MKAKGTIRES LDWTNARRYF
YWRVRRRLAE EYIRRRMTIA SKTQTRDDQT ATLKAWFGRD TVHASEAELT QIWEHEDRVV
LEWFEGQSRK VDALIQELTA AGTAEEVVRM YTSDRAGVVE GFDRILQSLS DQEKQDILAK
FATMTV
//
