ID A0A163LUL8_DIDRA Unreviewed; 2209 AA.
AC A0A163LUL8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:KZM28136.1};
GN ORFNames=ST47_g723 {ECO:0000313|EMBL:KZM28136.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM28136.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM28136.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM28136.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
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:KZM28136.1}.
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DR EMBL; JYNV01000033; KZM28136.1; -; Genomic_DNA.
DR STRING; 5454.A0A163LUL8; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000076837; 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; 2.
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:UP000076837}.
FT DOMAIN 57..493
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 189..253
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 304..369
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 620..694
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1445..1787
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1791..2106
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2209 AA; 245877 MW; FBE881DBF38C9EEF CRC64;
MASAAHHGAT GSDANGAPSS YAAQFELAPH FIGGNQLSAA APGKVKDFVA ANDGHTVITN
VLIANNGIAA VKEIRSVRKW AYETFGDERA IQFTVMATPE DLQANAEYIR MADQYVEVPG
GTNNNNYANV ELIVDVAERM NVHAVWAGWG HASENPKLPE SLAASPKKIV FIGPPGSAMR
SLGDKISSTI VAQHAQVPCI PWSGTGVNEV EVDSQGIVTE GLEAARKIGF PVMVKASEGG
GGKGIRKVER EDEFEQLYKA AASEIPGSPI FIMKLAGSAR HLERRHQKII EEAPVTVAGS
KTFQEMEKAA VSLGRLVGYV SAGTVEYLYS HADDKFYFLE LNPRLQVEHP TTEMVTGVNL
PAAQLQIAMG LPLHRFSTAG SAQNQRRPTP KGHCTACRIT SEDPDEGFKP SGGTIHDLNF
RSSSNVWGYF SFGHIFAYGE NRQASRKHMV VALKELSIRG DFRTTVEYLI KLLETPAFED
NTITTGWLDE LITKKLTAER PDPMIAVISG AVTKAHVASE ACISEYKTSL EKGQVPSKDV
LKTVFPIDFI YEGFRYKFTA TRSTLDSFTL FINGSKVSVG LRALADGGLL ILLGGKSHNV
YWKEEVGATR LSVDGKTCLL EQENDPTQLR TPSPGKLVKF TVENGDHIAK GQPFAEVEVM
KMYMPLIAQE DGIVNLIKQP GATLEAGDIL GVLALDDPSK VKSAQNFLGL LPDMGMPQVM
GSKPPQRVAY LSGVLQNILQ GFDNQVIMQS TLKELVEVLR DPELPYGEWN AQASALHARM
PQKLDITLGQ IVEKAHSRQL EFPSKQLSKA FDKFLAENVA KGDADLLKAG LAPLLDVISR
YSEGLKAHEY SVVLQYLEQY WATERLFSSR NSRDEEVILK LRDENRDNIA SVVHTVLSHT
RVSAKNNLVI AILDLYRPNR PGVGNIAKYF KDTLKKLTEL ESRQTAKVSL KAREVLIQCA
MPSLEERTAQ MEHILRSAVV ESRYGESGWD HREPNFEVIK EVVDSRYTVF DVLTQFFVHQ
DPWVALAALE VYTRRAYRAY QLQNINYHNE GEQQCLLSWD FVLRKVGEAE YGLAVEPSEP
GTPSTPAFER PPRIHSMSDL SAWNARFENE PSRKGVVAPV EYLDDADESL AKALELFPSV
GAYKKGGVSL KDGLSLKRTP TSGVNAPKQN TDELTGVLNV AVRDIEGVND EEILERILPI
VEEYKEELLA RRIRRLTFIC GHKDGTYPGY YTFRGPSYEE DDSIRHVEPA LAFQLELGRL
SKFNIKPVFT ENRNIHIYEA VGKGAESDKR YFLRAVVRSG RLREEIPTAE YMVSETDRLM
TDILDALEIV GTSQADMNHI FINFSHVFPL NPTEVEEAIG GFLERFGRRL WRLRVTGAEI
RIIVTDPQTG IPYPLRVIIT NTSGYVIQVE MYAERKSEKA GKWLFHSIGG TTKIGALHLQ
PVTTAYPTKG ALQPKRYKAH LMGTQYVYDF PELFRQATEN SWTAAIAKHA YLRDKQPPKG
DCVEYFELVL DDNDNLAEVN RDPGNNIIGM VGWIVTAKTP EYPRGRRFII IANDITFKIG
SFGPQEDKFF HKCSELARKL GIPRIYLSAN SGARIGLAEE LIPHFSVAWK DADRPEAGFD
YLYLTPEKYQ HFVDGKRNDV ICEKVEESGE TRYKITTIIG QEDGLGVESL RGSGLIAGET
SRAYEDIFTI TLVTCRSVGI GAYLVRLGQR AIQIEGQPII LTGAQAINKL LGREVYTSNL
QLGGTQIMYR NGVSHMTADD DFEGVSKIVK WMSYVPDKKG SPVPISPTAD DWDRDVTYFP
PNKAAYDVRH LIAGKEDADG FLSGLFDRGS FEESLGGWAK TVVVGRARLG GIPVGVIGVE
TRSVENVTPA DPANPDSIEQ VTSEAGGVWY PNSAFKTAQA IKDFNNGEQL PLMILANWRG
FSGGQRDMYN EVLKYGSYIV DALVKFEQPI FVYIPPYGEL RGGSWVVVDP TINPQYMEMY
ADVDSRGGVL EPEGIVGIKY RRERQLETMA RNDPTYGALK RKLNDPATAQ DQLQSIKAEM
TKREELLLPI YGQIAIQFAD LHDRSGRMEA KGVIRQALRW QNARRFFYWR LRRRLNEEYI
LKKLASAASP SQENPKPDAV TRATSMEMLK AWSQVPQFEN DDMSVATWYE ENRKTVHERV
EKLKTDGIAL EIANLMRRDR EGGLKGVVSL LSTLPTGEKE EVLKMLNRA
//
