ID A0A059J926_TRIIM Unreviewed; 2305 AA.
AC A0A059J926;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KDB23987.1};
GN ORFNames=H109_04092 {ECO:0000313|EMBL:KDB23987.1};
OS Trichophyton interdigitale (strain MR816).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB23987.1, ECO:0000313|Proteomes:UP000024533};
RN [1] {ECO:0000313|EMBL:KDB23987.1, ECO:0000313|Proteomes:UP000024533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR816 {ECO:0000313|EMBL:KDB23987.1,
RC ECO:0000313|Proteomes:UP000024533};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Trichophyton interdigitale MR816.";
RL Submitted (FEB-2014) 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:KDB23987.1}.
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DR EMBL; AOKY01000281; KDB23987.1; -; Genomic_DNA.
DR STRING; 1215338.A0A059J926; -.
DR HOGENOM; CLU_000395_5_1_1; -.
DR OMA; PTPKGHC; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000024533; 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:UP000024533}.
FT DOMAIN 52..560
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 204..401
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 687..761
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1513..1855
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1859..2174
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1211..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2179..2217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2179..2193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2305 AA; 256006 MW; C5B80ED31D0FD8E4 CRC64;
MPESNSTAVN GYGSAYAAKH NLPSHFIGGN RLDLAPPGAV KDFVAKNDGH SVITSVLIAN
NGIAAVKEIR SVRKWAYETF GDERAIQFTV MATPEDLRAN ADYIRMADQY VEVPGGTNNN
NYANVELIVD VAERTGVHAV WAGWGHASEN PKLPESLAAS PRKIIFIGPP GNAMRSLGDK
ISSTIVAQHA GVPCIPWSGT GVDEVKVDEE GIVTVEDSVY DQGCTHSPEE GLKKAREIGF
PVMVKASEGG GGKGIRKVDS EENFEALYNA AASEIPGSPI FIMKLAGNAR HLEVQLLADQ
YGNNISLFGR DCSVQRRHQK IIEEAPVTVA KQTTFQEMEK AAVRLGRLVG YVSAGTVEYL
YSHADDKFYF LELNPRLQVE HPTTEMVTGV NLPAAQLQIA MGLPLHRIRD IRLLYGVDPN
TSSPIDFGFS NEESTMVQRR PQPKGHTTAC RITSEDPGEG FKPSSGTMHE LNFRSSSNVW
GYFSVGTAGG IHSFSDSQFG HIFAYGENRS ASRKHMVVAL KELSIRGDFR TTVEYLIKLL
ETPAFEDNTI TTGWLDELIT KKLTAERPDP MVAVICGAMT KAYLASEACE SEYRKGIEKG
QVPAKDVLST VFPIDFIYEG SRYKFTATRS SIDSYHLYIN GSKCTVGVRA LADGGLLILL
DGRSHNVYWK EEAAATRLSV DGKTCLLEQE NDPTQLRTPS PGKLVKFTIE NGEHIRAGEA
FAEVEVMKMY MPLIAQEDGV VQFIKQPGAT LEAGDILGIL ALDDPSRVKH ASPFTGQLPE
LGPPQVLGNK PPQRFMVLLK ILQDILLGYD NQVIMGSTLN ELVQVLRNPE LPYGEWNAYA
SALHSRMPQK LDAQMTQVID RAKARKADFP AAQLLKTVTR FIDENVKAAA DAEALRTTIA
PLLQIIERYK DGLKVQEYKI IVSLLEQYWE VERLFAQGNT RDESVILKLR DENKDDISKV
IQIVLSHSKI GSKNNLILAI LDMYRPNKPN VGNVANYLKA ILRKLAELES RATAKVALKA
REVLIQCALP SLEERVAQME HILRSSVIES KYGETGWDHR EPDLNVLKEV VDSKYTVFDV
LPLFFAHNDQ WVSLAALEVY VRRAYRAYAL KGIEYHNTGD APFFVSWDFV LRKVPHSEFG
LSAQSTTSSV PGTPISEINP FKKIGSISDM AFANKGSDEA TRKGVLIPVH YLDEAEEVLY
KALSVFPRST PAAAKPKKNG TLPDRSRPAP RSEPDEELSG VCNVAIRDVE DLDDSELSSR
LTALVNDAKS ELLARGIRRL TFVCGHEDGT YPGYFTFRGP TYAEDVSIRH SEPALAFQLE
LGRLSKFKIK PVFTENRNLH VYEAIGKGPE LSDNAVDKRY FTRAVVRPGR LRDDIPTAEY
LISEADNLMT DILDALEIIG NNNSDLNHIF INFTPVFPLQ PVDVEKALAG FLERFGRRLW
RLRVTGAEIR ILCTDPATGT PYPLRVVITN TSGYIIQVEL YVERKSEKGE WIFHSIGGTT
KIGSMHLRPV STPYPTKEWL QPKRYKAHLM GTQYVYDFPE LFRQAFQNSW TTAIAAHPAL
AEKRPALGTC IEYSELVLDD RDNLAEVSRE PGTNTHGMVG WLITAKTPEY PRGRRFIVVA
NDITYQIGSF GPQEDKFFYQ CTELARKLGI PRIYLSANSG ARIGMADELM SQFNVAWNNP
EKPESGFKYL YLTPEVEKRL EKEKKKDLIT ELITEDGEER YKITTIIGAK DGLGVECLRG
SGLIAGATSK AYEDIFTITL VTCRSVGIGA YLVRLGHRAI QVEGQPIILT GAPAINKLLG
REVYTSNLQL GGTQIMYKNG VSHMTANDDF AGITKIVEWM SFVPEKKGAP IPVRPSSDPW
NRDITYCPPP KQPYDVRWII GGKEDDEGFL SGLFDKGSFE EALGGWARTV VVGRARLGGI
PMGVIAVETR SVDCVTPADP ANPDSMEVLS TEAGGVWYPN SAFKTAQALK DFNNGEQLPV
MILANWRGFS GGQRDMYNEV LKYGSYIVDA LVKYEQPIFV YIPPHGELRG GSWVVIDPTI
NPDQMEMYAD VEARGGILEP EGIVNIKYRR DKQLDTMARL DPEYGALRES LKDKSHSPEK
LSEIKAQMTE REERLLPVYM QIALQFADLH DRAGRMEAKG TIRQPLEWKN ARRFFYWRLR
RRLSEEIILK RMAAATVSSA TSSQASSSPP SSPIPTHSDA PPRVNASSIT TPRTQRDENL
DKLKAWTGIS DDEFESNDRE VAIWYEENKK NVYEKIEALK TDGIAAEVAS LLMGNKEGGL
RGVQKVLSML PDTEKAAVLK YLGSS
//
