ID A0A445C9V3_ARAHY Unreviewed; 2263 AA.
AC A0A445C9V3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RYR47623.1};
GN ORFNames=Ahy_A07g033568 {ECO:0000313|EMBL:RYR47623.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR47623.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR47623.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738}, and
RC GDAAS-fuhuasheng2018 {ECO:0000313|EMBL:RYR47623.1};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR47623.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) 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}.
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:RYR47623.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SDMP01000007; RYR47622.1; -; Genomic_DNA.
DR EMBL; SDMP01000007; RYR47623.1; -; Genomic_DNA.
DR STRING; 3818.A0A445C9V3; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000289738; Chromosome a07.
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; 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; 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}; Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738}.
FT DOMAIN 38..545
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 675..749
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1500..1839
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1843..2158
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2263 AA; 252541 MW; 2AAD91574D822265 CRC64;
MAGVGRGNGY TNGVVPNRHP ATISEVDEYC NALGGTRPIH SILIANNGMA AVKFIRSVRS
WAYETFGTEK AILLVAMATP EDMRINAEHI RIADQFVEVP GGTNNNNYAN VQLIVEMAEI
TRVDAVWPGW GHASENPELP DALKAKGIVF LGPPAVSMAA LGDKIGSSLI AQAAEVPTLP
WSGSHVKIPP DSCLVTIPDE IYREACVYTT EEAIASCQVV GYPAMIKASW GGGGKGIRKV
HNDDEVRALF KQVQGEVPGS PIFIMKVASQ SRHLEVQLLC DQYGNVAALH SRDCSVQRRH
QKIIEEGPIT VAPPQTVKLL EQAARRLAKS VNYVGAATVE YLFSMETGEY YFLELNPRLQ
VEHPVTEWIA EINLPAAQVA IGMGIPLWQL PEIRRFYGVE HGGGNDAWRK TSALATPFDF
DKAQSTKPKG HCVAVRVTSE DPDDGFKPTS GKVQELSFKS KPNVWAYFSV KSGGGIHEFS
DSQFGHVFAF GESRALAIAN MVLGLKEIQI RGEIRTNVDY TIDLLNASDY RDNKIHTGWL
DSRIAMRVRA ERPPWYLSVV GGALYKASAS SAALVSDYVG YLEKGQIPPK HISLVHSQVS
LNIEGSKYTI DMVRGGSGSY RLRMNQSEVE AEIHTLRDGG LLMQASILDG NSHVIYAEEE
AAGTRLLIDG RTCLLQNDHD PSKLVAETPC KLMRYLVVDD SHIDADTPYA EVEVMKMCMP
LLSPASGVIH FKMSEGQPMQ AGELIARLDL DDPSAVRKAE PFNGKFPVLG PPTATSDKVH
QKCAASLNAA QMILAGYEHN IDEVVQSLLN CLDSPELPFL QWQECFAVLA NRLPKDLKNE
LESKYKEYER ISSFQVVDFP AKLLKGILEA HLSSCPNKEK GAQERLIEPL LSLVKSYEGG
RESHARKIVQ SLFEEYLFVE ELFSDNIQAD VIERLRLQYK KDLLKIVDIV LSHQGIKSKN
KLILRLMDKL VYPNPAAYRD QLIRFSQLNH TNYSQLALKA SQLLEQTKLS ELRSNIARSL
SELEMFTEDG ENIDTPKRKS AINDRMEDLV SAPLAVEDAL VGLFDHSDHT LQRRVVETYI
RRLYQPYLVK GSVRMQWHRS GLIASWEFLE EYIERKSGVE DQMSDKTLVE KHTEKKWGVM
VVIKSLHFLP AIITAALKEA TNNLHEAVSS AAGEPVKHGN MMHVALVGIN NQMSLLQDSG
DEDQAQERIN KLAKILKEEE VGSTIRGTGV GVISCIIQRD EGRTPMRHSF HWSAEKLYYQ
EEPLLRHLEP PLSIYLELDK LKGYENIRYT PSRDRQWHLY TVMDQKPQPV QRMFLRTLLR
QPTTNEGFSS YQRTDAETPS TELAMSFTSR SIFRSLMAAM EELELNSHNA TIRPEHAHMY
LYIIREQEIN DLVPYPKRVD IDAGQEETTV EATLEELAHE IHSSVGVRMH RLGVVVWEVK
LWMAACGQAN GAWRIVVNNV TGHTCTVHIY REMEDTNTHR VVYSSITVKG PLHGVPVNET
YQPLGVIDRK RLSARKNSTT FCYDFPLAFE TALEQSWAIQ QPGFRRPKDK NLLKVTELRF
ADKEGSWGTP LVPVEHSAGL NDVGMVAWFM DMCTPEFPSG RTILVVANDV TFKAGSFGPR
EDAFFRAVTD LACAKKLPLI YLAANSGARL GVAEEVKACF KVGWSEESNP EHGFQYVYLT
PEDFARIGSS VIAHELKLES GETRWIIDTI VGKEDGLGVE NLSGSGAIAG SYSRAYKETF
TLTYVTGRTV GIGAYLARLG MRCIQRLDQP IILTGFSALN KLLGREVYSS HMQLGGPKIM
ATNGVVHLTV SDDLEGVSAI LKWLSYIPSH VGGSLPIVKP LDPPERPVEY LPENSCDPRA
AISGTLDGNG RWLGGIFDKD SFVETLEGWA RTVVTGRAKL GGIPVGIVAV ETQTVMQIIP
ADPGQLDSHE RVVPQAGQVW FPDSATKTAQ AIMDFNREEL PLFILANWRG FSGGQRDLFE
GILQAGSTIV ENLRTYKQPI FVYIPMMGEL RGGAWVVVDS RINSDHIEMY ADRTAKGNVL
EPEGMIEIKF RTRELLECMG RLDQKLITLK AKLQEAKDKR DTESFESLQQ QIKSREKQLL
PLYTQIATKF AELHDTSLRM AAKGVIRQVL DWGNSRAVFY RRLYRRIGEQ SLINNVREAA
GDHLSHVSAM DLVKNWYLSS NIAKGRKDAW LDDEAFFSWK ENPLNYEDKL KELRAQKVLL
QLTNIGDSVL DLQALPQGLA ALLSKLEPSS RVKLTEELRK VLG
//
