ID A0A0Q6FW02_9ACTN Unreviewed; 1864 AA.
AC A0A0Q6FW02;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Fused acetyl/propionyl-CoA carboxylase subuit alpha/methylmalonyl-CoA decarboxylase subunit alpha {ECO:0000313|EMBL:KQT93956.1};
GN ORFNames=ASG49_03140 {ECO:0000313|EMBL:KQT93956.1};
OS Marmoricola sp. Leaf446.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Marmoricola.
OX NCBI_TaxID=1736379 {ECO:0000313|EMBL:KQT93956.1, ECO:0000313|Proteomes:UP000051542};
RN [1] {ECO:0000313|EMBL:KQT93956.1, ECO:0000313|Proteomes:UP000051542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf446 {ECO:0000313|EMBL:KQT93956.1,
RC ECO:0000313|Proteomes:UP000051542};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT93956.1, ECO:0000313|Proteomes:UP000051542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf446 {ECO:0000313|EMBL:KQT93956.1,
RC ECO:0000313|Proteomes:UP000051542};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:KQT93956.1}.
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DR EMBL; LMRF01000001; KQT93956.1; -; Genomic_DNA.
DR STRING; 1736379.ASG49_03140; -.
DR OrthoDB; 3754062at2; -.
DR Proteomes; UP000051542; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
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 CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR013537; AcCoA_COase_cen.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
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; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR Pfam; PF08326; ACC_central; 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; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 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}; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000051542}.
FT DOMAIN 18..471
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 144..342
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 598..681
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1581..1864
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1545..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1864 AA; 200087 MW; 9495FE8D2FEB2974 CRC64;
MRDQPRIPSV QPEGSFVSFR RIAIVNRGES AMRLLHAVRE LNAARHPDDH LQTVALHTTG
EANAMFVREA DLAHDLGPAS QRPYVDLAVL ERALLETGAD AIWPGWGFVA EDPAFVDLCD
KHGVTFVGPS AEAMRRLGDK IGSKLIAEQV GVPVAPWSRG AVDTLEDALV AAEQVGYPLM
LKATAGGGGR GIRMVASAAD LEDAYQRTSD EALRAFGNGT VFLERLVTGA RHVEVQLIAD
SHGTAWALGV RDCSIQRRNQ KVIEESASPL LSPAQVEELK TAAEQLALAV GYVGAGTVEF
LYHPGEQTFA FLEVNTRLQV EHSITEATTG IDLVRAQLHV AQGGRLEGEK PAEVGHAVEA
RLNAEDPDRD FAPAPGRIEH LELPSGPGIR VDTGVAEGDT IPPDFDSMIA KIIAYAPTRD
EALARLRRAM TSTTVVIEGG ACNKSFVLDL LAQPEVVSGD PEHGLPWADT GWIDRVRAEG
RLASHAHAGV AVVAAGIEAY LERVRLETAR LIETAHGGRP SAAHEVGRPV ELKLRGVPYQ
VSTINTGPGR FRVGVASGAT SQTVDVQLAH VDDVRRRLTV GGRRYHVVTA THGPTTLVEV
DGVAHRVSRD EGGVLRSPAP ALVVATPVAV GDEVEAGATV VVLESMKMET ALHAPFPARV
KELHVITGSQ VETGAALIKL EQLGEGTEEV ADAGPGIDLP ADAGVDPATQ RERARAALSA
VVLGYDVPPE DQDAALSEYL TVRDLAEPDD GSVLADEVTL LETFVDLAEL SRNRPADEDR
HTALRVHSSR EHFHTYLLSL DADRGGLPEQ FRERLQRVLR HYGLASLDRT PELEAAVFRI
FLAQQRTTPE VALVGALLGA WSREAPPVGD LAARSREVLE RLGRVPQARY PAVGDLARSV
RFRWFDQPAV DAERSGVLLG MRDEVEALAA SADAPDRARR IEALASIPEQ TVGFLCDRLE
HGVPEREPML EVLARRHYRE YDLHDVRSID VPRPVVVAGY SVDDRPTRLV SSLGSVAELV
DGSELVTAVS SHLADRAGED AVVDLYLSWP DAPASVDEAS EQLRALFDAL PLTQDVRRVC
VAVCSGGGDR RVGYYTFRPA TDVEDGSAAA GAGVVEDDLT RGVHPMVGRR LDLWRLRNFH
VTRIEAPEDV LLYECVAREN PSDRRLVALA QVRQMSVVRD DDGTITGLPH AERAVESCLE
SIRRERVARG RGGARLDLNH VWVHVWPVVD LDLDALGALG AKISPLTDGA GVEEVVAQGR
LAVPGADPVP MAVRFSARPG SGVTSTVEEP PTELLQPLDD YTSKVVRSRR RGLVYPYELS
GVLAGPGGSL VEHDLDETGR LVPVDRPYGL NESGILAAVV RTPTPLHPDG VTRVVLCGDP
TKSLGSVAEQ ECLRVIAALD LAEEMQVPVE WFALSAGARI SMDSGTENMD WVAKALRRIV
EFTQDGGEIN VVVAGINVGA QPYWNAEATM LMHTKGILVM TPESAMVLTG KQSLDFSGGV
SAEDNYGIGG YDRVMGPNGQ AQYWAPDLAG AFGVLMAHYE HTYVAPGESG PRRTDSGDPV
DRDISSFPHE VEGSDFSTVG EIFSATANPD RKKPFDIRTV MRAVADQDHD VLERWAGMAD
ADTAVVQDAH VGGYPVCLLG IESQSVRRSG FPPTDGPSTY TSGTLFPKSS KKAARAINSA
SGNRPLVVLA NLSGFDGSPE SMRNLQLEYG AEIGRAIVNF RGPIVFCVIS RYHGGAFVVF
SKALNPAMTV LAVEGSFASV IGGAPAAAVV FTGEVEKRTA ATPAVKALDE RIAAARGAER
IGLQVERAQL RTAVRAEKIS EVAAEFDGIH DIHRAVEVGS VDAVIPAARL RPEIVEAIER
YVAS
//
