ID A0A428NBU7_9HYPO Unreviewed; 2283 AA.
AC A0A428NBU7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RSL38258.1};
GN ORFNames=CEP53_015025 {ECO:0000313|EMBL:RSL38258.1};
OS Fusarium sp. AF-6.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL38258.1, ECO:0000313|Proteomes:UP000287544};
RN [1] {ECO:0000313|EMBL:RSL38258.1, ECO:0000313|Proteomes:UP000287544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL38258.1,
RC ECO:0000313|Proteomes:UP000287544};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
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:RSL38258.1}.
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DR EMBL; NKCJ01000814; RSL38258.1; -; Genomic_DNA.
DR STRING; 1325737.A0A428NBU7; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000287544; 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:UP000287544}.
FT DOMAIN 62..570
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 220..411
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 697..771
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1522..1860
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1864..2179
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1220..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2283 AA; 255850 MW; D16F87DEE14B64C6 CRC64;
MTEISAGAQE GANGRSVPYV NGKASYAEKF NIADHFIGGN RVENAPPSKV KDFVVQNGGH
TVITNVLIAN NGIAAVKEIR SVRKWAYETF GDERAIHFTV MATPEDLQAN AEYIRMADHY
VEVPGGTNNH NYANVELIVD IAERMNVHAV WAGWGHASEN PKLPESLAAS PKKIVFIGPP
GSAMRSLGDK ISSTIVAQHA DVPCIPWSGT GVSDVAIDDK GIVTVADDIY AKGCVTSWEE
GLEKAKEIGF PVMIKASEGG GGKGIRKAEA EEGFEALYKA AASEIPGSPI FIMKLAGNAR
HLEVQLLADQ YGNNISLFGR DCSVQRRHQK IIEEAPVTIA KPDTFKAMEE AAVRLGKLVG
YVSAGTVEYL YSHADDKFYF LELNPRLQVE HPTTEMVSGV DLPAAQLQIA MGLPLHRIRD
IRLLYGVDPK TSSEIDFEFK NEGTALSQRR PQPKGHTTAC RITSEDPGEG FKPSNGVMHE
LNFRSSSNVW GYFSVGSQGG IHSFSDSQFG HIFAYGENRS ASRKHMVMAL KELSIRGDFR
TTIEYLVKLL ETEAFEENTI STGWLDELIS KRLTAERPET MLAVVCGAIT KAHIASEACM
AEYRAGLEKG QVPSKDILKT VFTIDFIYEG FRYKFTATRA SSDSYHLFIN GSKCSVGVRA
LSDGGLLILL DGRSHNVYWK EEVGATRLSV DNKTCLLEQE NDPTQLRSPS PGKLVKYTVE
NGAHVRAGQT YAEVEVMKMY MPLVAQEDGV VQLIKQPGAT LEAGDILGIL ALDDPTRVKQ
AQAFVDKLPA YGEPVVIGSK PAQRFSVLYN ILNNILLGYD NSVIMLPTLK ELIEVLRDPE
LPYSEWNAQF SALHARMPQK LDAQFTQIVD RAKSRHAEFP AKSLGKAFHR FLEDNVAPAD
TDMLKTTLAP LTEVIDMYSE GQKNRELSVI KGLLEQYWEV ENLFMNQPQE DAVVLKLRDQ
HKDDIMKVVH TVLSHSRVSA KSSFVLAILE EYRPNKPKAG NIAKNLRDTL RMLTELQSSR
PTSKVSLKAR EIMIQCSLPS LEERTAQLEH ILRTSVIESR YGETGWDHRE PSLDIIKEVV
DSKYTVFDVL TMFFAHDDPW VSLASLEVYV RRAYRAYILK SIEYHQDESD SPLFVSWDFQ
LRKLGQSEFG LPLQSAAPST PATPSGGEFN FKRIHSISDM SYLTHKWEDE PTRKGVIVPC
KYIDDAEDLI GKALETLATE QRQRKKHTTP GLIPDLSGKR KPVQAKQEPE ELSAVINVAI
RDSESRDDRE TLERILPIVE QYKDELLARA VRRLTFICGH SDGSYPGYYT FRGPEYKEDD
SIRHSEPALA FQLELARLAK FHIKPVFTEN KSIHVYEGIG KAVDTDKRYF TRAVIRPGRL
RDEIPTAEYL ISEADRVVND IFDALEIIGN NNSDLNQVFI NFTPVFQLQP KEVEESLQGF
LDRFGIRAWR LRIAQVEIRI ICTDPQTGTP YPLRVVITNT SGYVVDVDMY AERKSEKGEW
VFHSIGGTHE KGPMHLLPVS TPYATKNWLQ PKRYKAHLMG TQYVYDFPEL FRQAIQNTWT
KAVKIQPSLA SQQPKSGDCI SFTELVLDDK DNLDEVNREP GTNTCGMVGW IFRARTPEYP
NGRRFIVIAN DITYKIGSFG PKEDDFFHKC TELARKLGIP RIYLSANSGA RLGLADELMG
HFKVAWNDVN NQQGGFRYLY LDEETKTRFE KDVITEEVSE DGEKRHKIVT IIGKEEGLGV
ECLRGSGLIA GATSRAYNDI FTVTLVTCRS VGIGAYLVRL GQRAVQIEGQ PIILTGAPAL
NNLLGREVYT SNLQLGGTQI MYRNGVSHMT ANDDFAGISK IVEWMSFVPE KRNSPVPVSP
SVDDWDRDIT YFPPQKQPYD VRWMIGGREG EDGFESGLFD KDSFVEALGG WAKTVVVGRA
RLGGIPMGVI AVETRSVENI TPADPANPDS IEQVSNEAGG VWYPNSAFKT AQAINDFNNG
EQLPLMILAN WRGFSGGQRD MYNEVLKYGS FIVDALVKYE QPIFIYIPPF GELRGGSWVV
VDPTINPTAM EMYADVEARG GVLEPEGIIG IKYRKDKQVK TMARMDPEYA GLKKQLEDLS
LSTEETDEIK KKMAIREKQL LPVYAQIAVQ FADLHDRAGR MKAKGVIRDS LEWVNARRYF
YWRLRRRLNE EYIIRRMTST IISTSHSQTA AKNAETRAKY LHLLRSWSGI VDWEKDDQAV
TEWYETERKT IGEKVDALKS EVLAAEVASV VRGHAKAGWT GVREVLRVMP VEEREQILKY
LQQ
//
