ID A0A1Q4WS58_9ACTN Unreviewed; 1825 AA.
AC A0A1Q4WS58;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Fused acetyl/propionyl-CoA carboxylase subuit alpha/methylmalonyl-CoA decarboxylase subunit alpha {ECO:0000313|EMBL:OKI12963.1};
GN ORFNames=A6A08_16050 {ECO:0000313|EMBL:OKI12963.1};
OS Nocardiopsis sp. TSRI0078.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1718951 {ECO:0000313|EMBL:OKI12963.1, ECO:0000313|Proteomes:UP000185866};
RN [1] {ECO:0000313|EMBL:OKI12963.1, ECO:0000313|Proteomes:UP000185866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0078 {ECO:0000313|EMBL:OKI12963.1,
RC ECO:0000313|Proteomes:UP000185866};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI12963.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LWLB01000036; OKI12963.1; -; Genomic_DNA.
DR RefSeq; WP_073705097.1; NZ_LWLB01000036.1.
DR STRING; 1718951.A6A08_16050; -.
DR OrthoDB; 5166719at2; -.
DR Proteomes; UP000185866; 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}.
FT DOMAIN 1..452
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 572..655
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1541..1821
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1825 AA; 197813 MW; 5931FD683F8B39DE CRC64;
MFSRIAIVNR GEAAMRLIHA VRDVAAETGT RIETVALYTD VDRTSTFVRE ADIAYDLGPA
SARPYLDLEV LERALVETGA DAAWVGWGFV AEDPAFAELC ERIGVTFVGP SAEAMRRLGD
KIGAKLIAEE VGVPVAPWSR GAVQTLDEAL AAADGIGYPL MLKATAGGGG RGIRVVTNEA
ELTDAYERTS QEAARAFGSG VVFLERLVTG ARHVEVQVIA DGEGTAWALG VRDCSVQRRN
QKIIEESASP VLAPSQTAEL KASAERLAVA VGYRGAATVE FLYHPGDEMF AFLEVNTRLQ
VEHPITESTT GFDLVRAQLH VASGGRLEGE PPVERGHAVE ARLNAEDPDR DFAPSPGRIV
RLDLPAGPGI RVDTGVSEGD TIPADFDSMI AKIIAYGRDR DEALGRLRRA MAQTTVVIAG
GATNKSFVLD LLDRPEVIDA SADTGWIDRV RGEGGLVSHR HSAVALAAAA IEAYEEEERA
ERQRLLSTAF GGRPQVQHQS GRPLDLKLRG VGYRVRVARV GAHRFRVGVE AGGEARTADV
ELDRFDRYAG RITVNGVRYR LLTDTHGPVH LVEVDGVTHR VSRDEGGVLR SPTPALVVAT
PLEVGAEVEA DAPVLVLESM KMETVLRAPF RARLKECAVS VGSQVETGAP LLRLEPLADG
GDTEAAPAAG SVELDLPSAT GEAPARERLA RGREDLRSLL LGFDVDPHDE LRVLDDYLAA
RRTATEDGHR PLAEELELVG VLTDLAELSR NRPAGEDGGG DAHVHSPREY FHTYLQSLDV
ERAGLPESFQ AKLARALGHY GVTDLERSPE LEAAVFRIFL AQQRASADAT VVTALLRAWL
GEPPPDEALR EPAGLVLERL VAATQVRFPV VADLARGVVF SWFGQPLLRR NRARVYADVR
RHLRHLDANP DAPDRAERIA EMVRSTEPLV RLLGQRLVRE DLDNAVMLEV LTRRYYGNKG
LTGVRTSEVA GCTFVVAERA GSRVASTAVG FEALGSALRG LAELANGEDA VDADIYLAWE
KQPEDSDAMA TALNEVLSVH PLPDRVRRLT ATVAGRDGAV MHHHFTFRPS DTGMAEDRLI
RGLHPYIAQR MQLERLSKFD LTRLPSSDEE VYLFRCVARE NPSDDRLVAF AQVRDLTELR
EHDGRLIALP TAENTIATCL DSIRRAQAQR PPRKRSNTNR IVVYVWPPID ITREELETIG
RRVLPTTTGA GLEEILFIAR QRDRRTGELA KVAVRVSFDA AGGVELTVGE PSDEPVEPVD
DYRQKVLRAS SRNTVYPYEL TGLLGDFVEH DLDDDHVLVP VDRPKGRNTA AIVAGVVTTP
TREHPQGVTR VVLLGDPTKS LGALSEPECR RVIAALDLAE RMRVPLEWYA LSAGARISME
SGTENMDWVA AALKRIVEFT QDGGEINIVV AGINVGAQPY WNAEATMLMH TKGILVMTPD
SAMVLTGKQS LDFSGGVSAE DNFGIGGYDR VMGPNGQAQY WAPNLTAARD VLMSHYAHSY
IAPGEEAPRR ARTSDPADRD ISGFPHAVEG SDFTTVGEIF SAETNPDRKK PFDIRTVMRA
LADQDHPVLE RWAGMADAET ATVQDVHLGG MPVCLLGIES RSVPRRGFPP TDGPDTYTAG
TLFPRSSKKA ARAINAASGN RPLVVLANLS GFDGSPESMR KLQLEYGAEI GRAIVNFQGP
IVFCVISRYH GGAFVVFSKA LNPNMTVLAL EGSFASVLGG APAAAVVFSG EVNARTAADP
RVRDLEARVA AASGAERAAL TAELDELRSS VRVEKLGEVA AEFDRVHDIR RAVEVGSVDA
VIRAAELRPR VIEAIESRLR QGASR
//
