ID A0A2K1QFL0_9PEZI Unreviewed; 2298 AA.
AC A0A2K1QFL0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PNS13906.1};
GN ORFNames=CAC42_1397 {ECO:0000313|EMBL:PNS13906.1};
OS Sphaceloma murrayae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS13906.1, ECO:0000313|Proteomes:UP000243797};
RN [1] {ECO:0000313|EMBL:PNS13906.1, ECO:0000313|Proteomes:UP000243797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS13906.1,
RC ECO:0000313|Proteomes:UP000243797};
RA Cheng Q.;
RT "Draft genome sequence of a variant of Elsinoe murrayae.";
RL Submitted (JUN-2017) 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:PNS13906.1}.
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DR EMBL; NKHZ01000089; PNS13906.1; -; Genomic_DNA.
DR STRING; 2082308.A0A2K1QFL0; -.
DR InParanoid; A0A2K1QFL0; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000243797; 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; 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:UP000243797}.
FT DOMAIN 58..566
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 210..407
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 693..767
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1523..1865
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1869..2184
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 440..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2298 AA; 255169 MW; 8A7A7880A3B601B4 CRC64;
MADAVGGAAK VNGHTNGSPS SYAARFNLQP HFIGGNELSQ APHSKVKDFV AANDGHTVIT
NVLIANNGIA AVKEIRSVRK WAYETFGDER AIQFTVMATP EDLAANADYI RMADKYVEVP
GGTNNNNYAN VELIVDIAER MGVHAVWAGW GHASENPKLP ESLAASPNKI VFIGPPGSAM
RSLGDKISST IVAQHAKVPC IPWSGEGVDQ VRVDENGIVT VEDHIYDKGC VHNHEEGLIA
AKKIGFPVMV KASEGGGGKG IRKVENEEDF EQLYKAAASE IPGSPIFIMK LAGSARHLEV
QLLADQYGNN ISLFGRDCSV QRRHQKIIEE APVTIANQTT FQAMEKAAVS LGRLVGYVSA
GTVEYLYSHA DDKFYFLELN PRLQVEHPTT EMVSGVNLPA AQLQVAMGLP LHRIRDIRLL
YGADPRTSTE IDFDFSKEGS KINQRRPQPK GHTTACRITS EDPGEGFKPS SGKMHDLNFR
SSSNVWGYFS VGAASSIHSF SDSQFGHIFA YGENRQASRK HMVVALKELS IRGDFKTTVE
YLIKLLETPA FEDNTITTGW LDELISKKLT AERPDPMIAV ICGAVTKAHL ASEECINTYR
QSLEKGQVPS KDVLKTVFPV DFIYEGMRYK FTATRSSIDS YTLFINGSKC AVGIRPLSDG
GILTLLSGRS HSVYWKEEVG ATRLSVDSKT CLLEQENDPT QLRTPSPGKL VKFTIENGQH
VKKGQPFAEV EVMKMYMPLI AQEDGIVNLI KQPGATLQAG DILGILALDD PTKVKSAQPF
LGQLPDFGPP QIVGNKPPQR FTFLYNILRD ILSGFDNQVI MAETLKELVA VLRDPELPYG
EWNAQASALH ARMPQKLDTQ LSQIVDRAHS RGTEFPAKQL QRAFARFLEE NLPAGDAATL
RTSLEPLLTI MTKYADGLKA NEFGVFITLF NQYYAVENLF SARQNRDDEV ILSLRDQNKD
KVADIVHTVL SHTRVSTKNN LVQAILDTYR PNRPGVGNVA KYFRPSLKQL AELESRSTAK
VALKARELLI QCAMPSLEER TSQMEHILRS SVLESRYGES GWDHREPDFD IIKEVVDSKY
TVFDVLPHFF AHQDPYVSLA ALEVYTRRAY RAYQLKSIDY NTDVEAPFVL LWDFALRKVG
ASEFGLPVEA SHPSTPGTPA STDGFSRINS FSDLSKFKDA DAPSRRGAVV PVQYLDEVDE
ALTKALESIP TSGPTKKRGS ESGTLMADLT KKRSQTASAP PAAQEKENTD DLTAVVNIAV
RDAESLVDQE ILQRIMPIVA DFKTELYARK VRRLTFICGH KDGTYPGYFT FRGPSYAEDE
SIRHIEPALA FQLELSRLSK FHIKPVFTEN RNIHIYEATG KGAENDKRYF TRAVVRPGRL
REDISTAEYM ISEADRLMTD ILDALEIIGN NNSDMNHIFI NFSAVFPLQP KEVEEALAGF
LDRFGRRAWR LRVTGAEIRL IVTDPNTGEP YPLRVIITNT SGYIIEVELY AERKTEKGNE
WVFNSIGGTT KIGSMHLRPV STPYATKGAL QPKRYKAHIM GTQYVYDFPE LFRQAVENSW
KTVVVQHPHL KDKQPKQGEC IEYSELVLDD TDSLAEVNRD PGTNTIGMVG WIVTARTPEY
PRGRRFIIIA NDITFKIGSF GPQEDKFFHK CSELARKLGI PRVYLSANSG ARIGMAEELI
PHFSVAWRNP DRPEAGFDYL YLTPDKKARF EDGALKHVIT KEVKVGSETR HVITTIVGAE
DGLGVECLKG SGLIAGETSR AYEDIFTVTL VTCRSVGIGA YLVRLGQRAI QIEGQPIILT
GAPAINKLLG REVYTSNLQL GGTQIMYKNG VSHMTANDDF EGVSKILKWL SFVPDKKGSP
VPISPSADAW DRDITYFPPQ KQPYDVRWLI GGKSDDEGYL SGLFDRGSFE ESLGGWARTV
VVGRARLGGI PVGVIGVETR SVENVTPADP ANPDSIEQVT QEAGGVWYPN SAFKTAQAIR
DFNNGEHLPL MILANWRGFS GGQRDMYNEV LKYGSYIVDA LVKFEQPIFI YIPPFGELRG
GSWVVVDPTI NPQFMEMYAD EDARGGVLEP EGIVGIKFRK ERQLETMARL DATYGGLKAK
LADDSLSTEQ LGEIKNQMTA RERLLLPVYA QISLQYADLH DRAGRMKAKD AIRAPLVWKN
ARRFFYWRLR RRLNEEHLLK RMASAAPKDI SHPTAAAAAG SSASAETMGI RKSNLTQLAA
WTGINGFENE DQKVALWYEE NRKVVHEKIE RIRTESVAYD VASLLRGSKE GGLRGVRDVL
QMLPVGEREE VLKFLGAA
//
