ID A7EM01_SCLS1 Unreviewed; 2285 AA.
AC A7EM01;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDO03867.1};
GN ORFNames=SS1G_06348 {ECO:0000313|EMBL:EDO03867.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDO03867.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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 EMBL; CH476628; EDO03867.1; -; Genomic_DNA.
DR RefSeq; XP_001592109.1; XM_001592059.1.
DR STRING; 665079.A7EM01; -.
DR GeneID; 5488792; -.
DR KEGG; ssl:SS1G_06348; -.
DR VEuPathDB; FungiDB:sscle_13g092240; -.
DR InParanoid; A7EM01; -.
DR OMA; PTPKGHC; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; 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:UP000001312}.
FT DOMAIN 59..567
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 211..408
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 694..768
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1519..1861
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1865..2180
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2285 AA; 254273 MW; 7427FEB084A8B397 CRC64;
MADQHTNGTV PIISSTNGGG SSYAARHNLA DHFIGGNKLE NAPASKVKDF VAASDGHTVI
TNVLIANNGI AAVKEIRSVR KWAYETFGDE KAIQFTVMAT PEDLQANADY IRMADQYVEV
PGGTNNNNYA NVELIVDVAE RMNVHAVWAG WGHASENPKL PESLAASPKK IVFIGPPGSA
MRSLGDKISS TIVAQHAKVP CIPWSGTGVD KVEVNEDGIV TVEDEVYKKG CIQSWEEGLE
KAKEIGFPVM IKASEGGGGK GIRKAESEQG FEALYKAAAS EIPGSPIFIM KLAGNARHLE
VQLLADEYGN NISLFGRDCS VQRRHQKIIE EAPVTVAKQA TFQAMEKAAV RLGRLVGYVS
AGTVEYLYSH SDDKFYFLEL NPRLQVEHPT TEMVSGVNLP AAQLQIAMGL PLHRIRDIRL
LYGVDPSTTT EIDFDFSQEK SIQTQRRPTP KGHTTACRIT SEDPGEGFKP SSGTMHELNF
RSSSNVWGYF SVGTAGGIHS FSDSQFGHIF AYGENRSASR KHMVVALKEL SIRGDFRTTV
EYLIKLLETP AFEDNTITTG WLDELISNKL TAERPDPMLA VVCGAVTKAH IASEACISEY
RTSLEKGQVP SKDILKTVFP IDFIYDGHRY KFTATRSSLD SYHLFINGSK CSVGVRALSD
GGLLVLLSGR SHNVYWKEEV GATRLSVDSK TCLLEQENDP TQLRTPSPGK LVKFTVENGE
HIKAGQAFAE VEVMKMYMPL IAAEDGIVQL IKQPGATLEA GDILGILALD DPSRVKHAQP
FLGHLPDLGP PQIVGTKAAQ RFVLLRNILN NILDGFDNQV IMGSTLKELI EVLRDPELPY
GEFNAQFSAL HARMPQKLDA TLTQILDRSK ARNAEFPAKN LSKALQKFLD ENVAPADVDL
LTASLAPLIE ILNRYQNGPK AHEFAVFSGL LQKYASVERL FSGRTSRDEE VILKLRDENK
DDIAKVVQTV LSHSRVGAKN NLILAILEEY RPNKPNAGDV AKYLRAPLKS LTELESRQTA
KVSLKAREIL IQCALPSLEE RAAQMEHILR SSVVESRYGE TGWEHREPDL EVLKEVVDSK
YTVFDVLPIF FGHSDPWVSL AALEVYIRRA YRAYSLQKIE YHNESADPPF IVSWDFVLRK
VGASEFGMPI QSSAPSTPAT PSYESGNPFK RISSISDMTY LTNKPDHEPT RKGVIVPVQY
LDEAEEYLQR ALEVFPVAGG KKKGNGLLPE LGGKRKVAPP RLDTEDELTA VCNVAIQDAE
SLDDNETVAK IKLIVNDYKE ELLNRRIRRL TFICGHKDGS YPGYYTFRGP NYEEDESIRH
SEPALAFQLE LGRLSKFKIT PVFTENRNIH IYEAVGKEAT SDKRYFTRAV VRPGRLRDEI
PTAEYLISES DRLMNDILDA LEIIGNNNSD LNHIFINFSP VFPLQPPEIE QALGGFLERF
GRRLWRLRVT GAEIRIICTD PSTGMPYPVR VVITNTSGYV IQVEMYAERK SEKGGEWVFQ
SIGGTTKIGS MHLRPVSTPY PTKEWLQPKR YKAHLMGTQY VYDFPELFRQ AIQNSWVKAV
RKHSSLADKQ PPTGECIEYS ELVLDDNDGL AEVLREPGTN THGMVGWLVT AKTPEYPRGR
KFVIVANDIT FRIGSFGPKE DQFFHKCTEL ARKMGIPRIY LSANSGARIG MAEELMPHFK
VAWKNPERQE AGFKYLYLDT DTKKRFEDGK SKDVITEEVV EDGETRHKIV TIVGAEDGLG
VECLKGSGLI AGATSRAYED IFTITLVTCR SVGIGAYLVR LGQRAIQIEG QPIILTGAPA
INKLLGREVY TSNLQLGGTQ IMYKNGVSHM TANDDFEGVS KIVEWMAYVP DKRNSPLPIG
PAADSWDRDI VYTPPEKQPY DVRNIIAGKE DDEGFMSGLF DKDSFVESLG GWAKTVVVGR
ARLGGIPMGV IAVETRSVEN ITPADPANPD STEQISNEAG GVWYPNSAFK TAQAIKDFNN
GEQLPLMILA NWRGFSGGQR DMYNEVLKYG SYIVDALVKY EQPIFVYIPP FGELRGGSWV
VVDPTINPEY MEMYADEDAR GGVLEPEGIV NIKYRKDKQL ETMARLDPEY AELKKQLLDN
SLGQEKLSEV KLRVEQREKA LLPVYNQISL QFADLHDRAG RMKAKGVIRE SLKWREARRF
FYWRVRRRVN EEYILKRMLS ANSKSPNGTR PENLRKLAAW TAIPAFETDD KSVAMWYEEN
RKVVHEKVEH LKIEGVAAEV ATLLRASGPG AKGGLSGGAM AGIRQVLSML PVEEREEALK
FLGRS
//
