ID G5EAT9_EMENI Unreviewed; 2288 AA.
AC G5EAT9; C8V2D1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBF70132.1};
GN ORFNames=ANIA_06126 {ECO:0000313|EMBL:CBF70132.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF70132.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; BN001301; CBF70132.1; -; Genomic_DNA.
DR RefSeq; XP_663730.1; XM_658638.1.
DR SMR; G5EAT9; -.
DR STRING; 227321.G5EAT9; -.
DR EnsemblFungi; CBF70132; CBF70132; ANIA_06126.
DR GeneID; 2871063; -.
DR KEGG; ani:AN6126.2; -.
DR VEuPathDB; FungiDB:AN6126; -.
DR eggNOG; KOG0368; Eukaryota.
DR HOGENOM; CLU_000395_5_1_1; -.
DR InParanoid; G5EAT9; -.
DR OMA; DFEDNTI; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000000560; Chromosome I.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; ISA:AspGD.
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; ISA:AspGD.
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:UP000000560}.
FT DOMAIN 51..559
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 203..400
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 686..760
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1511..1853
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1857..2172
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2288 AA; 255182 MW; 927E2518811EB1AB CRC64;
MGVPDGTTNG HGGSRAAKHN LPSHFIGGNH LDAAAPSSVK DFVANHEGHS VITSVLIANN
GIAAVKEIRS VRKWAYETFG NERAIQFTVM ATPEDLAANA DYIRMADQYV EVPGGTNNNN
YANVELIVDV AERMDVHAVW AGWGHASENP RLPESLAASP KKIIFIGPPA SAMRSLGDKI
SSTIVAQHAQ VPCIPWSGTG VDEVKVDENG IVTVEEEVYN KGCTFSPEEG LEKAKQIGFP
VMIKASEGGG GKGIRKVEKE EDFINLYNAA ANEIPGSPIF IMKLAGNARH LEVQLLADQY
GNNISLFGRD CSVQRRHQKI IEEAPVTIAN PTTFQAMERA AVSLGKLVGY VSAGTVEYLY
SHADDKFYFL ELNPRLQVEH PTTEMVTGVN LPAAQLQIAM GIPLHRIRDI RLLYGVDPNT
SAEIDFDFSS EESFKTQRRP QPKGHTTACR ITSEDPGEGF KPSSGTMHEL NFRSSSNVWG
YFSVGTAGGI HSFSDSQFGH IFAYGENRSA SRKHMVIALK ELSIRGDFRT TIEYLIKLLE
TPAFEENKIT TGWLDQLISN KLTAERPDTT IAVLCGAVTK AHQASEARLE EYRNGIQKGQ
VPSKDVLKTV FPVDFIYEGK RYKFTATRAG LDSYHLFING SKCSIGVRAL ADGGLLVLLN
GRSHNVYWKE EAAATRISVD GKTCLLEQEN DPTQLRTPSP GKLVKFTVEN GEHVRAGQPF
AEVEVMKMYM PLIAQEDGIV QLIKQPGATL EAGDILGILA LDDPSRVKHA QPFTEQLPPI
GPPQVVGNKP AQRFFLLHSI LENILKGFDN QVIMNSTLKE LIEVLRDPEL PYSEWNAQSS
ALHSRMPQKL DAQLQNIVDR ARSRKAEFPA RQLQKTMVRF IEENVNPADA EILKTTLLPL
VQVINNYIEG LKAHEYKVFV GLLEQYYAVE KLFSGSKARY EDGILALREE HKDDVATIVQ
IALSHSRIGA KNDLILAILS IYRPNQPGMA NVGQYFKSIL KKLTEIESRA AAKVTLKARE
VLIQCALPSL EERLSQMELI LRSSVAESQY GETGWAHREP DLGALKEVVD SKYTVFDVLP
RFFVHKDAWV TLAALEVYVR RAYRAYSIQG IQYHHEGEPA FLSWDFTMGK LGQPEFGSMT
AVTHPSTPST PTTESNPFKR VSSISDMSNL LNDSPNGTPR KGVILPVQYL EDAEEYLTKA
LEVFPRAGTR KPSDHGLIAS LEGKRRPAPR ADSESTELTG VLNIAIRDIE ELDDAQIVAQ
ISKLVSSFKD EFLARRIRRV TFICGKDGVY PSYYTFRGPN YEEDESIRHS EPALAFQLEL
NRLSKFKIKP VFTENRNIHV YEAIGKGPEN DKALDKRYFV RAVVRPGRLR DDIPTAEYLT
SEADRLMNDI LDALEVIGNN NSDLNHIFIN FSPVFNLQPK DVEEALAGFL DRFGLRLWRL
RVTGAEIRIL CTDPATGMPY PLRVIISNTV GYIIQVELYI EKKSEKGEWL LHSIGGTNKL
GSNHLRPVST PYPTKEWLQP KRYKAHVMGT QYVYDFPELF REAFQNSWTK AIEKSPSLIE
RRPPLGECME YSELVLDDTD NLVEISRGPG TNTHGMVGWI VTARTPEYPE GRRFIIVAND
ITFQIGSFGP LEDKFFHKCT ELARKLGIPR VYLSANSGAR IGMADELIPY FSVAWNDPAK
PEAGFKYLYL TPEVKKKFDA SKQKEVITEL IHDEGEERHK ITTIIGAKDG LGVECLKGSG
LIAGATSRAY EDIFTITLVT CRSVGIGAYL VRLGQRAIQV EGQPIILTGA PAINKLLGRE
VYTSNLQLGG TQIMYRNGVS HMTAANDFDG VEKIVDWLAF VPEKKGSLPP IRPLADPWDR
DVSYHPPAKQ AYDVRWLING KEDEEGFLPG LFDAGSFEEA LGGWARTVVV GRARLGGIPM
GVIAVETRSV ENVTPADPAN PDSMEMITQE AGGVWYPNSS FKTAQALRDF NNGEQLPVMI
LANWRGFSGG QRDMYNEVLK YGSYIVDALV KYEQPIFVYI PPFGELRGGS WVVVDPTINP
DQMEMYADEE ARGGVLEPEG IVNIKFRRDK QLETMARLDP TYGELRRALQ DKNLSKEKLS
DIKDKMAARE EQLLPVYMQI ALQFADLHDR AGRMQAKNTI RQALSWKNAR RFFYWRVRRR
ISEEYIIKRM LTACPAPVQG EGSGAVAQGV SPAPSDSPRT THLRTLHSWT PFLENEVEND
DRRVAVWYEE NKELIQEKIE ALKSQAIASQ ISDVLFSNRE SGLKGIQQAL SFLPVEEKES
ILKYLGSN
//