ID A0A1V9ZPK7_9STRA Unreviewed; 2274 AA.
AC A0A1V9ZPK7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:OQR99927.1};
GN ORFNames=THRCLA_06330 {ECO:0000313|EMBL:OQR99927.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQR99927.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQR99927.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQR99927.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQR99927.1}.
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DR EMBL; JNBS01001774; OQR99927.1; -; Genomic_DNA.
DR STRING; 74557.A0A1V9ZPK7; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000243217; 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: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:UP000243217}.
FT DOMAIN 35..536
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 189..385
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 666..740
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1503..1847
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1853..2166
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1128..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2274 AA; 253107 MW; 76A061CC1F9FC751 CRC64;
MAAEPTSLRK ARADSRVLTF TSMAQYVEEL QGRRPVTKML IANNGISAVK AIRSIRKWAY
ETFGNERMVQ FFVMATPEDL RANAEYIRMA EHVIEVPGGS NNNNYANVML IVELAERFEV
DAVWAGWGHA SENPLLPDSL AKTKRKIIFV GPSGKPMRAL GDKIGSTIIA QSAHVPTIAW
NGDGITVNYK KLNMIPDEIY QSASIRDVDH CVEQCDRIGF PVMIKASEGG GGKGIRKITR
REDVVAGYTA VQGEIPGSPI FVMKLAPKSR HLEVQLLADE YGNAIALSGR DCSVQRRHQK
IIEEGPVLAP TEAVWDEMML AATRLAKEVD YVNAGTVEYL FTESPDKDGN NFFFLELNPR
LQVEHPVTEM ITGVNLPACQ LQVAMGIPLH MIPDIRRLYN KDSFGKTKID FDTEKQNPPH
GHVIAARITA EDPNAGFQPT SGAIEELNFR STADVWGYFS VDSSGRVHEY ADSQIGHLFS
WSTSRERARK NLALALKELS IRGEINTTVE YLVGLIETDD FKNNRISTSW LDERIARHKE
LSTHGRPDTL MVVLVGAMCL AYQASNSRLE KYVAQLERGQ IPSPELLAQE DSLELIYEGI
KYKIKAARSG AITFTLYCND SYVQADIRTL SDGGYLVLLN GKSHVAYATK EAQGLRLIVD
GNTCVFTNEY DPTRLVTNAA GKLARYLVKD GAKLRRGTPY AEVEVMKMYM PLLTPEDGVV
RHVKPEGAVL APGDLIATME LDDPSCVKLS DVYLGKLPAF SNEPENASAK SCFVLKKAME
IVGTLLEGYV APADLVQKAL TDLFKALEDP LLPVEELGEV LSSLAGRIPG AVYDDIFELK
TRFRNSDKSV PFDMSKVVTV IENFKSKIAS VADVNAFEGK IAPLRDVISK YSAGLKSRRE
HAIHELIAKY YTVEQVYAQT MNMEDIIMAL RNAHTGNLSC VFGIARAHLA VDRRSKCLLD
ILQHIHQGAK DSNASYVPML EAIANFRGRN YSLVSLEARR ILIDRKMPSY AERLLEMEQL
LLTIVKDPKP DHETVPFQKL LDQPQPVFDL LISLLNHKDD RVRDCALNLY IRRIYRTYEI
SKMDLHQSSN FLVEKFEFKS PVDPAAAVKG SIPKADSYND LASLLKKGSS SPNLVSLSRS
DSTGSDSDSS LTKSVGRSIP SNVNRHGLMA AFENLADFKK HFPSLLEMVP KRNMLSGIKT
SDFVHVLHII LLTQEATEEK TLAQLQEVVR GIKDALTNRL VRRITFAVKP RLNVNIDNTS
TYHLYPGIYT FRQNMQYEED AIVRHMEAPL AYRLELQRLG NYNVVTVDSK DKNVHLYLAT
PKKSALVAAK AGKNDVFQRF FVRAVVRQLE RLDDTVSSTF DAHPGPERTL VDALNVLELA
MGSNITDPSM PIKNNHVYMN VAPEAVVDPQ YLEAVIRILA SRYADRLAQL RVSQVELKIG
AKFNDNAYSI PVRLVASNPT GYVLRVEAYV EAQEMQNGTE VNIFSSIGDD VVGELDGLPV
STPYPVTYAF DAKREAAKRS SDTIYAYDFL ELIEHALARN WRKFASDRAK QRIATKIPNK
FLEAKEFILT NGDNEVELVT RPRGQNDVGM VAWLITLYTP ELPSGRQLVL ISNDITFNAG
SFGTREDKLF DLASKYARAA GVPRLYFAAN SGARIGMAET IKAKYNVAWK DASDPSKGFE
YLYLTKADYD YFNSVKAVQG KELVLPSGEV RYVITDIIGE EKDLGVENLK GSGCIAGESS
RAYQDIFTLT YVCGRSVGIG AYLVRLGQRT VQNVSNAPII LTGYQALNKL MGNNVYTSND
QLGGIKIMHN NGVTHLTSSN HIQGIASILN WLSFVPAVRG GSLPIRDIAG VDSIDRPITF
TPTRVAYDPR ELLTGKIMDS TWHSGFFDKD SFVETLSAWA KTVVVGRGRL GGIPCGVVVT
EVRTVEKLTP ADPASPTTQE SLVQQAGQVW FPDSAHKTAT AIRDFNTEDL PLFIFANWRG
FSGGQRDMFD EVLKFGAEIV DGLVSYKQPV FVYIPPFAEL RGGAWVVVDP TINADCMEMY
ADPQGRGGVL EPAGLIEIKY RKPALLATAH RVDATLIRLD AQLAALAEND DTRNGIVREI
RLREAKLLPI FTQIATHFGD LHDTPGRMKA KEVIRDVVAW SNARVYFYWR LKRRLEEFRV
RRSILNSSNE EMSKGFGATE ATLQSWFEEQ NKGENWSDDR AVLSWLTRDG DWIAKKLEAL
NQERIAREVT RLGLQDPNAA VVGILHMISE LPAANRDEVI TALRRGSIFA RSTN
//
