ID A0A453GLS1_AEGTS Unreviewed; 2233 AA.
AC A0A453GLS1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:AET3Gv21106200.19};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET3Gv21106200.19, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET3Gv21106200.19}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
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 EnsemblPlants; AET3Gv21106200.19; AET3Gv21106200.19; AET3Gv21106200.
DR Gramene; AET3Gv21106200.19; AET3Gv21106200.19; AET3Gv21106200.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000015105; Chromosome 3D.
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; 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:UP000015105}.
FT DOMAIN 26..515
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 178..372
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 642..716
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1470..1812
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1816..2137
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2233 AA; 248266 MW; 13092B3FF08283AA CRC64;
MVESDQINGR MSSVDEFCKA LGGDSPIHSV LVANNGMAAV KFMRSIRTWA LETFGNEKAI
LLVAMATPED LRINAEHIRI ADQFLEVPGG TNNNNYANVQ LIVEIAERTR VSAVWPGWGH
ASENPELPDA LMEKGIIFLG PPSAAMGALG DKIGSSLIAQ AAGVPTLPWS GSHVKVPQET
CHSIPEEIYK NACVSTTDEA VASCQVVGYP AMIKASWGGG GKGIRKVHND DEVRALFKQV
QGEVPGSPIF IMKVASQSRH LEVQLLCDKH GNVAALHSRD CSVQRRHQKI IEEGPITVAP
PETIKELEQA ARRLAKCVQY QGAATVEYLY SMETGEYYFL ELNPRLQVEH PVTEWIAEIN
LPASQVVVGM GIPLYNIPEI RRFYGIEHGG GYHAWKEISA VATKFDLDKA QSVKPKGHCV
AVRVTSEDPD DGFKPTSGRV ESGGAIHEFS DSQFGHVFAF GESRSLAIAN MVLGLKEIQI
RGEIRTNVDY TVDLLNAAEY RENKIHTGWL DSRIAMRVRA ERPPWYLSVV GGALYEASSR
SSSVVTDYVG YLSKGQIPPK HISLVNLTVT LNIDGSKYTI ETVRGGPRSY KLRINESEVE
AEIHSLRDGG LLMQLDGNSH VIYAETEAAG TRLLINGRTC LLQKEHDPSR LLADTPCKLL
RFLVADGSHV VADTPYAEVE VMKMCMPLLL PASGVIHFVM PEGQAMQASD LIARLDLDDP
SSVRRAEPFH GTFPKLGPPT AISGKVHQKF AASVNSAHMI LAGYEHNINH VVQDLLNCLD
SPELPFLQWQ ELMSVLATRL PKDLRNELDA KYKEYELNAD FRKSKDFPAK LLRGVIEANL
AYCSEKDRVT SERLVEPLMS LVKSYEGGRE SHARAVVKSL FEEYLSVEEL FSDDIQSDVI
ERLRLQHAKD LEKVVYIVFS HQGVKSKNKL ILRLMEALVY PNPSAYRDQL IRFSALNHTA
YSGLALKASQ LLEHTKLSEL RTSIARSLSE LEMFTEEGER ISTPRRKMAI NERMEDLVCA
PVAVEDALVA LFDHSDPTLQ RRVVETYIRR LYQHYLVRGS VRMQWHRSGL IALWEFSEEH
IEQRNGQSAS LLKPQVEDPI GRRWGVMVVI KSLQLLSTAI EAALKETSHY GAGVGGVSNG
NPINSNSSNM LHIALVGINN QMSTLQDSGD EDQAQERINK LSKILKDNTI TSHLNGAGVR
VVSCIIQRDE GRSPMRHSFK WSSDKLYYEE DPMLRHVEPP LSTFLELDKV NLEGYNDAKY
TPSRDRQWHM YTLVKNKKDP RSNDQRMFLR TIVRQPSVTN GFLFGSIDNE VQASSSFTSN
SILRSLMAAL EEIELRAHSE TGMSGHSHMY LCIMREQRLF DLIPSSRMTN EVGQDEKTAC
TLLKHMVMNI YEHVGVRMHR LSVCQWEVKL WLDCDGQANG AWRVVVTSVT GHTCTVDIYR
EVEDPNTHQL FYRSATPTAG PLHGIALHEP YKPLDAIDLK RAAARKNETT YCYDFPLAFE
TALKKSWESG ISHVAESNEH NQRYAEVTEL IFADSTGSWG TPLVPVERPP GSNNFGVVAW
NMKLSTPEFP GGREIIVVAN DVTFKAGSFG PREDAFFDAV TNLACERKIP LIYLSATAGA
RLGVAEEIKA CFHVGWSDDQ SPERGFHYIY LTEQDYSRLS SSVIAHELKV PESGETRWVV
DTIVGKEDGL GCENLHGSGA IASAYSKAYR ETFTLTFVTG RAIGIGAYLA RLGMRCIQRL
DQPIILTGYS ALNKLLGREV YSSQMQLGGP KIMATNGVVH LTVSDDLEGV SAILKWLSYV
PPYVGGPLPI VKSLDPPERA VTYFPENSCD ARAAICGIQD TQGGKWLDGM FDRESFVETL
EGWAKTVITG RAKLGGIPVG IIAVETETVM QVIPADPGQL DSAERVVPQA GQVWFPDSAA
KTAQALLDFN REELPLFILA NWRGFSGGQR DLFEGILQAG SMIVENLRTY KQPAFVYIPK
AGELRGGAWV VVDSKINPEH IEMYAERTAR GNVLEAPGLI EIKFKPNELE ESMLRLDPEL
ISLNAKLLKE TSASPSPWET AAAAETIRRS MAARRKQLMP IYTQVATRFA ELHDTSARMA
AKGVISKVVD WEESRAFFYR RLQRRLAEDS LAKQVREAAG EQQMPTHRSA LECIKKWYLA
SQGGDGEKWG DDEAFFAWKD DPDKYGKYLE ELKAERASTL LSHLAETSDA KALPNGLSLL
LSKVSFFCLL VFV
//
