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Database: UniProt
Entry: Q2H8D2_CHAGB
LinkDB: Q2H8D2_CHAGB
Original site: Q2H8D2_CHAGB 
ID   Q2H8D2_CHAGB            Unreviewed;      1591 AA.
AC   Q2H8D2;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 102.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAQ91587.1};
GN   ORFNames=CHGG_03522 {ECO:0000313|EMBL:EAQ91587.1};
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ91587.1, ECO:0000313|Proteomes:UP000001056};
RN   [1] {ECO:0000313|Proteomes:UP000001056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC   {ECO:0000313|Proteomes:UP000001056};
RX   PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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   -!- 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; CH408030; EAQ91587.1; -; Genomic_DNA.
DR   RefSeq; XP_001230038.1; XM_001230037.1.
DR   STRING; 306901.Q2H8D2; -.
DR   GeneID; 4388561; -.
DR   VEuPathDB; FungiDB:CHGG_03522; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   HOGENOM; CLU_000395_5_1_1; -.
DR   InParanoid; Q2H8D2; -.
DR   OMA; DFEDNTI; -.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001056; 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; 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; 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; 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; 2.
DR   Pfam; PF21385; ACCA_BT; 1.
DR   Pfam; PF02785; Biotin_carb_C; 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; 1.
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; 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   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|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001056}.
FT   DOMAIN          1..416
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          79..257
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          543..617
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1327..1591
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1034..1053
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1591 AA;  177444 MW;  B63F6E6229902C9A CRC64;
     MAEPNGHANG PNGAAYAKGH ASENPKLPES LAASPKKIVF IGPPGSAMRS LGDKISSTIV
     AQHADVPCIP WSGTGVDEVS VDDKGIVTVP DDVYLKGCVN SWQEGLAKAE EIGFPVMVKA
     SEGGGGKGIR KVMDKENFEE LYKAAASEIP GSPIFIMKLA DSARHLEVQL LADQYGNNIS
     LFGRDCSPTT FKAMEDAAVR LGRLVGYVSA GTVEYLYSHA DDKFYFLELN PRLQVEHPTT
     EMVSGVNLPA AQLQVAMGLP LHRIRDIRLL YGVDPKTSTE IDFEFKNPES EKSQRRPTPK
     GHTTACRITS EDPGEGFKPS NGVLHDLNFR SSSNVWGYFS VGSAGGIHSF SDSQFGHIFA
     YGENRAASRK HMVVALKELS IRGDFRTTVE YLIKLLETDA FEQNTITTGW LDELISKKLT
     AERPDTMLAI VCGAVTKAHI ASESCIAEYR GGLEKGQVPA KDILKTVFPV DFIYEGFRYK
     FTVTRSSTDS YRLFINGSKC TVGVRALSDG GLLVLLNGRS HNVYWKEEVA ATRMSVDGKT
     CLLEQENDPT QLRSPSPGKL VKYSVENGAH VRSGQTFAEV EVMKMYMPLI AQEDGIVQLI
     KQPGAVLEAG DILGILALDD PSRVKQAQAF LGQLPQYGSP VVVGNKPSQI FSLKYNTLAN
     ILMGFDNQVV MLDTLKELIT VLRDDKLPYS EFSAQFSALH ARMPQKLDAQ FTQALDPPLT
     NILDLYADGQ KARELNVIAD LLSQYADVER LFSGRRLQDE EVILKLRDQN KDDIQKVVQT
     VLSHSRIAAK NSLVLAILDE YRPNKPNVGN VGKALRPVLR KLAELESRQT AKVSLKAREI
     LIQCALPSLE ERTAQMEHIL RSSVVESRYG ETGWDHREPN LEVIKEVVDS KYTVFDVLTL
     FFAHEDPWVS LAALETYVRR AYRAYNLKKI EYQTDETDTP AFVSWDFALR KIGQSEFGLP
     VQSAAPSTPA TPIDQTFSRI SSISDMSYLS QRARDEPVRK GVIIPCKYLD DAEDMLSRAL
     DTLPLLGNRR RSANPLTALN DRRRPAPPPR LDSMDELSAV VNVAVRDAEG RSDEDTLKDI
     LPLVEQFKED LFARRVRRLT FICGRNDGSY PAYYTFRGPH YIEDDSIRHI EPSLAFQLEL
     ARLSKFKIKP VFTENKNIHV YEGIGKDVET DRRFFTRAVI RPGRLRDEIP TAEYLISEAD
     RVINDIFDAL EIIGTSNSDL NHMFINFSPI FQLQPQEVEH SLQGFLDRFG PRGWRLRVAN
     VEIRIICTDP VTGQPYPLRV IITNTSGYVI QVEMYAERKS EKGEWVFHSI GGTTKIGAMH
     LLPVSTPYPT KNWLQPKRYK AHIMGTQYVY DFPELFRQAI QNSWATVTKA QPSLASEQPP
     TGECIDYNEL VLDDQDNLAE VSREPGTNSC GMVGWLIKAR TPEYPKGRRF IVVANDITYN
     IGSFGPKEDN FFFKCTELAR KLGIPRIYLS ANSGARLGLA NELMPHFSVA WNDAEKPEAG
     FKYLYLNDEA KRRFETEVIT EEVTEDGEKR HKIVTIVGAE DGLGVECLRG SGLIAGATSR
     AYNDIFTCTL VTCRSVGKFI SRSPRVLSHA I
//
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