ID K2SEA6_MACPH Unreviewed; 2273 AA.
AC K2SEA6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Carboxyl transferase {ECO:0000313|EMBL:EKG15200.1};
GN ORFNames=MPH_07647 {ECO:0000313|EMBL:EKG15200.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG15200.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG15200.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG15200.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG15200.1}.
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DR EMBL; AHHD01000324; EKG15200.1; -; Genomic_DNA.
DR STRING; 1126212.K2SEA6; -.
DR VEuPathDB; FungiDB:MPH_07647; -.
DR eggNOG; KOG0368; Eukaryota.
DR HOGENOM; CLU_000395_5_2_1; -.
DR InParanoid; K2SEA6; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000007129; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:UP000007129};
KW Transferase {ECO:0000313|EMBL:EKG15200.1}.
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 1517..1859
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1863..2178
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2273 AA; 253289 MW; C84E2A0A53F26114 CRC64;
MGLSADTGAQ ANGTPSSWAA KKNIGEHFIG GNHLGQAPPS KVKDFVASHD GHTVITNVLI
ANNGIAAVKE IRSVRKWAYE TFGDERAIQF TVMATPEDLQ ANADYIRMAD QYVEVPGGTN
NNNYANVELI VDVAERMGVH AVWAGWGHAS ENPKLPESLA ASPNKIVFIG PPGSAMRSLG
DKISSTIVAQ HADVPCIPWS GSGVDKVTVD ENGIVTVPDD VYDQGCTHSP EEGLEVARKI
GFPVMVKASE GGGGKGIRKV ESEENFIQMY RAAASEIPGS PIFIMKLAGN ARHLEVQLLA
DQYGNNISLF GRDCSVQRRH QKIIEEAPVT VANPETFQRM EKSAVALGKL VGYVSAGTVE
YLYSHEDDAF YFLELNPRLQ VEHPTTEMVS GVNLPAAQLQ IAMGIPLHRI RDIRLLYGVD
PHSATEIDFD FSTEESQINQ RRPKPKGHTT ACRITSEDPG EGFKPSSGTM HELNFRSSSN
VWGYFSVGTA GGIHSFSDSQ FGHIFAYGEN RTASRKHMVV ALKELSIRGD FRTTVEYLIK
LLETPAFEDN TITTGWLDEL ISKKLTAERP DPMVAVICGA VQKAHVASEQ CVTEYKNSLE
KGQVPSKEVL KTVFPIDFIY EGFRYKFTAT RSSSDAYTLF INGSRCQVGV RALADGGLLV
LLGGKSHNVY WKEEVGATRL SVDSKTCLLE QENDPTQLRT PSPGKLVKFT VENGQHISKG
QAFAEVEVMK MYMPLIAQED GVVNLIKQPG ATLEAGDILG ILALDDPSKV KSAQLFLGQL
PEFGPPQIMG NKPPQRFSYL YGVLQDILKG FDNQVIMADT LKELIAVLRD PELPYGQWNA
QASALHARMP QKLDSALSQI VDRAHSRGVE FPAKQLIKSF NRFLEESVDP ADASLLRSTL
APLFDVANLY VEGLKAHEFE VMASLLNQYC VVEHQFSYRQ NRDDEVILKL RDTQKDDLIP
VVYTVLSHTR VQSKNNLVLA ILDSYKPNQP GVGNVAKYMK EPLRKLTELE SRATAKVAIK
AREVLIQCAM PSLEERTTQM EHILRTSVVE SKYGESGWDH REPDFDIIKE VVDSKYTVFD
VLPTFFAHPD PYVALAALEV YTRRAYRAYQ LKQIDYHIET EPPYVLSWDF ALRKVGESEF
GLPVESSHPS TPSTPVSEQS SLFGKRIHSI SDMTYLRRST EGEPTRKGAV VPIPFLEDAE
EYLMRALECF PVHGSTKKRA SSGNNGLIAD LAGKRKPAPK LESEDELTAV CNVAVRDSES
FDDAEILDRI TPIVNDYKEE LLARRVRRVT FICGHKDGTY PGYYTFRGPS YEEDSSIRHI
EPALAFQLEL GRLSKFHIKP VFTENRNIHI YEAVGKGAEN DKRYFTRAVV RPGRLREGIP
TAEFMISEAD RLMNDILDAL QIIGNNGSDM NHIFINFSTV FPLQPLAVQE ALAGFLDRFG
RRAWRLRVTG AEIRIICTDE NGEPYPLRVV ITNTAGYVVD VELYAEKKSE KGGQWLFHSI
GGTTKIGSMH LRPVSTPYPT KGALQPKRYK AHIMGTQYVY DFPELFRQAI ENSWHLSCAK
NPALKEKQPV KGECIEYNEL VLDDNDNLAE VNREPGANTI GMVGWIVTAK TPEYPRGRKF
IIIANDITFK IGSFGPAEDK FFHKCSELAR KLGIPRIYLS ANSGARIGMA EELIPHFSVA
WNDPANPEKG FKYLYLTEEK KKHFEEGDRR DVITEEIEDE GEVRHKITTI VGAEDGLGVE
CLRGSGLIAG ETSRAYEDIF TITLVTCRSV GIGAYLVRLG QRAIQIEGQP IILTGAPAIN
KLLGREVYTS NLQLGGTQIM YKNGVSHMTA SDDFEGVSKI VRWLSFVPAS KGQPIPLSPT
PEHWDRDITY FPPQKQPYDV RWLIAGKEDE EGFLSGLFDR GSFEESLAGW ARTVVVGRAR
LGGLPVGVIG VETRSVENVV PADPANPDSI EQVTSEAGGV WYPNSAFKTA QAIRDFNNGE
QLPLIILANW RGFSGGQRDM FNEVLKYGSY IVDALVKYEQ PVFVYIPPFG ELRGGSWVVV
DPTINPQYME MYADEDARGG VLEPEGIVGI KFRKDRQLET MARLDQKYGE LKRKIADTSL
SKEEQQKVKQ EMTEREQLLL PVYAQISLQY ADLHDRAGRM AAKGTIRMPL RWQNARRFFY
WRLRRRINEE YILKKLSVSE SGAISRNEAL TQIRAWSGVE DFENNDQAVA EWIEANRKEV
AAKVENLTRE ATAFQVAELL RKDKDAGLKG VLAALEMLPT GEKEEILKKL TSA
//
