ID A0A176WL04_MARPO Unreviewed; 2243 AA.
AC A0A176WL04;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAE32916.1};
GN ORFNames=AXG93_399s1250 {ECO:0000313|EMBL:OAE32916.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE32916.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE32916.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE32916.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-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}.
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:OAE32916.1}.
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DR EMBL; LVLJ01000705; OAE32916.1; -; Genomic_DNA.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000077202; 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:UP000077202}.
FT DOMAIN 34..540
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 187..381
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 667..741
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1476..1813
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1817..2127
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2243 AA; 248411 MW; D3860A6248CE02FD CRC64;
MVVEASANGH AGSKHAAYVS QLEEYCFALG GTKPIHSILI ANNGMAAVKF IRSIRMWAYE
AFGVEKAVTL VAMATPEDMR INAEHIRMAD QFIEVPGGTN NNNYANIQLI VEIAERTGVS
AVWPGWGHAS EVPELPEQLA ARGIVFLGPP AEPMAALGDK IGSSIIAQAA GVPTMAWSGS
NVSIAFESCL EPIPDEVYRK ACVYTTEEAL ASCQIIGYPV MIKASWGGGG KGIRKVNSDD
EVRALFKQVQ GEVPGSPIFT MKVASQSRHL EVQLLADQFG NVAALHSRDC SVQRRHQKII
EEGPITVAPP ETIKALEQGA CRLAKSVNYV GAATVEYLFS METGEFYFLE LNPRLQVEHP
VTEWIAEFNI PAAQLCIGMG IPLWRMPEMR RFYGKTVGEG LPSWRDMATV EPFDFFTTEA
TKPKGHVVAV RVTSEDPDDG FKPTSGQVQE LSFRSKPNVW AYFSVKSGGG IHEFSDSQFG
HVFAYGETRP IAIANMVLGL KELHIRGEIR TNVDYTVDLL HDKEYRENNF HTGWLDSRIA
MRVRVERPPW NLSVVGGALY RGTMLTASRV LEYIGYLEKG QVPPKHISLV SFQVTLNIEG
YKYTVDMTKG GPGSYRLVLN QSEVEAEVHT LRDGGLLVQL DGNSHVVYAE EEAAGTRLLI
DGRTCLLQND HDPSRLIAET SCKLLRYLVA DGSHVNADAP YAEVEVMKMC MPLVTPASGT
IHCKMSEGST MAPGDLIAGL DLDDPSAVKK AVPFEGSFPP LGPPTAVAAK VHQRCAVADG
AARMVLAGYE HPIETVVQTL LTCLDDPVLP LYQWQEKMSI LGTRLPKNLK NKLDMEFREY
ETSFIDNKVV EFPAKSLKAA IEAAIAEVPE SDRSSIIRLV EPLVTLVKSY EGGRESHARS
TVKSLFDEYL RVEKLFSTDM QADVIEGLRQ TYKKDLPKVV DIVLSHQGVS RKNVLISRLM
GALVYPNPAA YREQLICFAE LSHPSQSELA LRSSQLLEQT KLSDLRANIA RSLSELEMFT
EEGGDGTQVP GRRRSAVEER MEDLVDAPLA VEDALVALFD HSDHTLQRRV VETYIRRLYQ
PYLVKGSIRM QWHRSGLIAS WQFMEENPQQ ANEKMSTLAP LEEERQGIRR WGTMAILTSL
HYLANAVGAA LKETGEAPKD AVNGSSREFG NIIHVALVGI KNQMSNLQDS GDEDQAQERV
DKIAKSLKSE SLGSMLTAAG VGIVSCIIQR DEGRSPTRHC FHWAPDQRFY EEEPLSRHVE
PPLSNLLELN KLKGFASMRY APSRDRQWHI YYVTDKPSNV KRTFLRTLVR QVKPSDNAGV
VDVAHATKNV EGSIQRILEE LELIVHDSNN KADHLHMYLS LLRPVEIGGA DTSGDDEDIE
QVDVVEKLKG LVHDIYKKLG ARMHRLAVWQ WEIRLRLTHA GCAIGAWRIV AQNPTGHTCT
VQVYKEVKNA VLGVVVYHSP LPASYGPLHG KPIATQHKPL DAVERRRLTA RRNNTTYCYD
FPLIFEKALE LAWLGSNSTK MGGSPIFKAT ELIFVDKKNY WNSSLVEVTR PVASNDVGMV
AWSIRMRTPE FPEGRAVFVV SNDVTYNVGS FGQKEDAFFK AVTDLAVQTK LPLIYLAANS
GARIGVSDEV RSSFRVGWSD ESSPDRGFQY LYLTPEDYQL ISTSVVSHEI QLPSGEVRWV
IDDIIGKEDG LGVENLSGSG AIAGAYSRAY QETFTLTYVS GRTVGIGAYL ARLGMRCIQR
SDQPIILTGF PALNKLLGRE VYSSHMQLGG PKVMAVNGVT HLTVADDLEG VSSILNWLSY
VPAVKGGPLP FLHATDPPQR LVEYTPETSC DPRAAIRGIE VDGKWLGGIF DKGSFVETLE
GWAQTVVTGR GRLGGIPVGI VAVETQTVMQ TIPADPGQPD SHERVVPQAG QVWFPDSAAK
TAQALLDFNK EGLPLFILAN WRGFSGGQRD LFEGILQAGS MIVEHLRTYK QPVFVFIPKT
GELRGGAWVV VDSKINVDQV EMYAERTAKG GVLEPEGLIE IKFREREIKE VINRLDSQVI
GLKQKMQAAD AQTALAITKQ ITARENKLLP LYKQIAIRFA ELHDTANRMA AKGVIKKPVE
WAQSRYFFHR RLKRRLVEEA LVRQVQDAAG DTLSHADALA LIKKWYLEAQ EPKFDYVAND
AVSDAWDDNR AFVAWGNQPC VMEEHLQGMR KERVSKELYA MAGTSSGNLK ALPEALRAML
QQVDEGSRNQ AVQELKTILE SFK
//
