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
//