ID C1GDJ1_PARBD Unreviewed; 2298 AA.
AC C1GDJ1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEH49248.2};
GN ORFNames=PADG_05327 {ECO:0000313|EMBL:EEH49248.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH49248.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH49248.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH49248.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN275962; EEH49248.2; -; Genomic_DNA.
DR RefSeq; XP_010760691.1; XM_010762389.1.
DR STRING; 502780.C1GDJ1; -.
DR GeneID; 22584276; -.
DR KEGG; pbn:PADG_05327; -.
DR VEuPathDB; FungiDB:PADG_05327; -.
DR eggNOG; KOG0368; Eukaryota.
DR HOGENOM; CLU_000395_5_2_1; -.
DR InParanoid; C1GDJ1; -.
DR OMA; PTPKGHC; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001628; 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:UP000001628}.
FT DOMAIN 54..562
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 206..403
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 689..763
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1516..1858
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1862..2177
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 433..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2182..2209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2298 AA; 257189 MW; 817A40B4BDD168DC CRC64;
MGVTDTPATA TNGFGSSFAA KHNLPSHFIG GNRLDLAPPG KVKDFVAKND GHSVITSVLI
ANNGIAAVKE IRDVRKWAYN TFGDERAIQF TVMATPEDLR ANADYIRMAD QYVEVPGGTN
NNNYANVELI VDIAERMGVH AVWAGWGHAS ENPKLPESLA ASPKKIIFIG PPGSAMRSLG
DKISSTIVAQ HAGVPCIPWS GEGIDDVTID EDGIVTVEDH IYDKGCTHSP QEGLEKARII
GFPVMVKASE GGGGKGIRKV DREEDFINLY NAAASEIPGS PIFIMKLAGN ARHLEVQLLA
DQYGNNISLF GRDCSVQRRH QKIIEEAPVT IAKPETFRAM ERAAVRLGKL VGYVSAGTVE
YLYSHADDKF YFLELNPRLQ VEHPTTEMVS GVNLPAAQLQ IAMGIPLHRI RDIRLLYGVD
PNTSSEIDFH FENEESTKTQ RRPKPKGHTT ACRITSEDPG EGFKPSSGTM HELNFRSSSN
VWGYFSVGTA GGIHSFSDSQ FGHIFAYGEN RSASRKHMVV ALKELSIRGD FRTTVEYLIK
LLETPAFEDN TITTGWLDQL ISNKLTAERP DPMIAVICGA VTRAHLSSEA CIAEYRKGIE
KGQVPSKDVL KTVFPVDFIY EGFRYKFTAT RSSNDNYHLF INGSKCSVGV RALADGGLLV
LLDGRSHNVY WKEEAAATRL SVDGKTCLLE EENDPTQLRT PSPGKLVKYT VENGEHVKAG
QPFAEVEVMK MYMPLIAKED GIVQLIKQPG STLEAGDILG ILALDNPSRV KHAQPFLGQL
PDLGPPQVVG NKPPQRFGLL HNILWDILRG FDNQVIMGAT LKELVEVLRN PELPYGEWNA
QVSALHSRMP QKLDSLLAQV VDRAKTRKAE FPANQLMKTL SRFIDDNVTP ADADILRTSL
QPLVDVIRRY SEGLKVHEYK VFIGILQQYW DVEHLFAGRN MRDEDVILKL REENKDDIFG
VIQTVLSHSK VGAKNNLLLA ILDMYRPNKP NAGNVGNYLK PILKKLAELE SRATSKVALK
AREVLIQCAL PSLEERVAQM EHILRSSVVE SKYGETGWDH REPDINVLKE VVDSKYTVFD
VLPLFFGHQD QWVSLAALEV YVRRAYRAYK LKGIEYHNQH ESPFFISWDF TLGKAGGQSD
FGMVAGSSHP STPTTPTMES NPFKKISSIS DMSYLVNKGV NEPMRKGVII PVNYLDDAEE
MLSRALEVFP RAESQKSSGS SITLSLAALR KPTPRVESID ELTGVCNVAI RDIEDLDDTE
MVSRITKLVS EVKEELLARR VRRLTFICGH KDGTYPGYFT FRGPTYNEDE SIRHSEPALA
FQLELGRLSK FRIKPVFTEN RNIHVYEAIG KGPESDKAVD KRYFTRAVVR PGRLRDDIPT
VEYLISEADN LMNDILDALE IIGNNNSDLN HIFINFTPVF PLQPADVERA LAGFLERFGR
RLWRLRVTGA EIRILCTEPT TGMAYPLRVV INNTSGYIIQ VEMYAERKSE KGEWIFQSIG
GTTKIGSMHL RPVSTPYPTK EWLQPKRYKA HLMGTQYVYD FPELFRQAFQ NCWTKASEEH
SSLADKRPAV GECIDYNELV LDDSDNLIEV AREPGTNTHG MVGWMITART PEYPRGRRFI
VIANDITFQI GSFGPQEDKF FHKCTELARK LGIPRIYLSA NSGARIGMAE ELMHHFSVAW
NDPERPEAGF KYLYLTPEVK KRLDERKTKN VITELVTENS EERHMITTVI GAEDGLGVEC
LRGSGLIAGA TSKAYEDIFT ITLVTCRSVG IGAYLVRLGQ RAIQVEGQPI ILTGAPAINK
LLGREVYTSN LQLGGTQIMY KNGVSHMTAN DDFEGIQKIV QWMSFIPDKK NSPVPIRPYS
DTWDRDIAYY PPARQTYDVR WLIAGKQDEE GFLPGFFDKD SFQETLAGWA RTVVVGRARL
GGIPIGVIAV ETRSVDTVTP ADPANPDSME LISTEAGGVW YPNSAFKTAQ ALKDFNFGEQ
LPVMILANWR GFSGGQRDMY NEVLKYGSYI VDALVKYQQP VFVYIPPFGE LRGGSWVVID
PTINPEQMEM YADEESRGGV LEPEGIVNIK YRRDKQLDTM ARLDPEYGEL RKALNDKFLP
ADQLSKIKAK MTEREEQLLP VYMQIALQFA DLHDRAGRMK AKETIRQALQ WKNARRFFYW
RLRRRLSEEL ILKRMAAAAP STTSRNSAVP NITATSPSSP LKPATPSRRD ANLNTLQSWT
GMLDREFDFN DRKVALWYEE NKKKVLENVE QMKVDGVAVE VAQLLMGNKD GGLRGVQQVL
SMLPVEEREA VLKYLGSP
//
