ID F8Q8W1_SERL3 Unreviewed; 2233 AA.
AC F8Q8W1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGN95016.1};
GN ORFNames=SERLA73DRAFT_77033 {ECO:0000313|EMBL:EGN95016.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(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; GL945486; EGN95016.1; -; Genomic_DNA.
DR STRING; 936435.F8Q8W1; -.
DR eggNOG; KOG0368; Eukaryota.
DR HOGENOM; CLU_000395_5_1_1; -.
DR InParanoid; F8Q8W1; -.
DR OMA; PTPKGHC; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000008063; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000008063}.
FT DOMAIN 38..546
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 190..387
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 673..747
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1472..1810
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1814..2128
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 2209..2233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2233 AA; 248099 MW; 5EC896A44719A04C CRC64;
MSAYDHSKAS QYIGGNSVDK APAGRVCDFV KANGGHTVIT KVLIANNGIA AVKEIRSIRQ
WSYETFGTER AVEFTVMATP EDLKVNAEYI RMADQYIEVP GGSNNNNYAN VDLIVDVAER
AGVHAVWAGW GHASENPRLP ESLSASKTKI VFIGPPGSAM RSLGDKISST IVAQSADVPT
MAWSGTGISD TVLSEQGFVT VPDKAYHDAC VTSVEEGLKK AEQIGWPVMI KASEGGGGKG
IRKVEEPDAF KNAYHAVAGE IPGSPIFIMK LAGQARHLEV QLLADQYGNA ISLFGRDCSV
QRRHQKIIEE APVTIAKQDT FEQMERAAVR LAKLVGYVSA GTVEYLYSHA EDVFYFLELN
PRLQVEHPTT EMVSGVNLPA AQLQIAMGIP LHRIRHIRTL YGVAPNASSE IDFDMVKPES
NQLQRKPRPK GHVVAVRITA ENPDAGFKPS SGSLQELNFR SSTNVWGYFS VATAGGLHEF
ADSQFGHIFA YGEDRGESRK NMIVALKELS IRGDFRTTVE YLIKLLELEA FKDNTITTGW
LDSLISSKLT AERPDATLAV VCGAVTKAHL ASDACLSEYK RILDKGQVPV RDLLKTVFGV
DFIYENVRYS FTATRSSKTM WTLFLNGGRT MVGARPLADG GLLVLLDGRS HSVYWREEVG
ALRLMVDAKT CLIEQENDPT QLRSPSPGKL IRFFIDSGDH IKAGEQYAEI EVMKMYMPLV
AAEDGIVQFV KQPGVSLEPG DILGILTLDD PARVKHAKPF EGLLPPMGSP GIAGNKAYQR
YLRCTGVLND ILEGYDNQAI MASTFKDLIE VIHDPELPYS EVNAILSALS GRMPFKLEDG
IRAAIEGAKS KGDGHEFPAV RIKKVLEHYV QDNILAHDRA MFRTQLSALY DVLERFMGGL
KGHEVHTLAT LLANYESTEK LFGGSIEARV LTLREQYKDE LDKVAGLVLS HTKAQSKSKL
VLALLDYVKS SGLPVSNPES RLYQVLNGLA ALESKSSTSV SLKAREVLIL GQMPSYEERL
IQMEAILKTS VTSNFYGEQG GANRTPSPEV LKELSDSRYT VYDVLPAFFS HTDPMVTLAA
FEVYVRRAYR AYSLLSIDYE EGDGVDDAEL PSALTWRFNL GQSHSPPATP RVTAGDPRRQ
GSVSDITYLI NRNQTQPVRN GVIASFSDLD ALAQCFEKIA SLLPLFDPEE FRQRYGNNQP
PNVMNLALRV FDEADDMAEE VWCEKLTEFV NCRNDSLQRR GVRRVTILIC RRGQYPLYFT
LREDNGVWVE EQAIRNIEPA LAFQLELSRL SNYKLTPCFV ETKQIHIYHS VAQENQLDNR
FFIRALVRPG RLRGTMSTAE YLVSETDRLV TSVLDALEVV SAQHRNADCN HIFMNFVYNL
VVTYDDVLEA ISGFIERHGK RLWRLHVTGS EIRISLEDSD GNVTPIRCII ENVSGFVVNY
HGYQEITTDK GTTILKSIGE KGPLHLQPVH LAYPTKESLQ PKRYQAHLIG TTYVYDFPEL
FSKALHNVWI KARKYDSSLV IPKKMLESKE LVLDEHDQIT EVERPPGNNA FGMVAWVYNL
KTPEFPKGRK VVVIANDITY KIGSFGPEED QFFYLVTKYA RTHGLPRIYL SANSGARIGL
AEETLSLFSC AWNDESHPEK GISYLYLTRQ NYLKLQEKGA GSVRTSEIDV DGETQYKITD
IIGLQDGLGV ESLRGSGLIA GETSRAYDDI FTITLVTARS VGIGAYLVRL GERAVQVEGQ
PIILTGAPAL NKVLGREVYT SNLQLGGTQI MHKNGVSHLT ASSDLEGVTH ILEWISYVPE
IRGAQLPVRE TLDPWDRDIT YMPPKGAYDP RWFIEGKTDE HTSEWLSGFF DKGSFQETLS
GWAQTVVVGR ARLGGIPMGV IAVETRTIER IVPADPANPA SFEQHVMEAG QVWYPNSAYK
TAQAIFDFNR EGLPLMIFAN WRGFSGGQQD MYDEVLKQGS KIVDGLSSYK QPVFVYIVPN
GELRGGAWVV LDPSINSEQM EMHADIDARA GVLEPEGIVE IKMRRDKILT LMERLDSTYA
SLKSDSKDAS KTAEERALAA QALAERETFL QPTYKQIALL YADLHDRTGR MEAKGCAKPA
VWKQARRNFY WALRAKLARS TALANIKETS PESSTEYRAK LLDSLISLED RSDNRSAALA
LEKLDLTPTL VKLRGDYLMH RFLEVAQQDR KATMDGLLRL VDSLSDDERS SLQSALQGNS
RSPGPPSYTN STI
//
