ID A0A136PV08_9ACTN Unreviewed; 1819 AA.
AC A0A136PV08;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Fused acetyl/propionyl-CoA carboxylase subuit alpha/methylmalonyl-CoA decarboxylase subunit alpha {ECO:0000313|EMBL:KXK62361.1};
GN ORFNames=AWW66_08975 {ECO:0000313|EMBL:KXK62361.1};
OS Micromonospora rosaria.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK62361.1, ECO:0000313|Proteomes:UP000070620};
RN [1] {ECO:0000313|EMBL:KXK62361.1, ECO:0000313|Proteomes:UP000070620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 803 {ECO:0000313|EMBL:KXK62361.1,
RC ECO:0000313|Proteomes:UP000070620};
RA Yang H., He X., Zhu D.;
RT "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT which can produce antibacterial substance rosamicin.";
RL Submitted (JAN-2016) 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:KXK62361.1}.
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; LRQV01000021; KXK62361.1; -; Genomic_DNA.
DR RefSeq; WP_067362608.1; NZ_LRQV01000021.1.
DR OrthoDB; 249215at2; -.
DR Proteomes; UP000070620; 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:UP000070620}.
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 1537..1819
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1819 AA; 197053 MW; BE57C3DB07F5A9EF CRC64;
MFSRVAIVNR GEAAMRLIHA VRELAAETGT RIETVALHTD VDRAATFVRE ADLSYDLGPA
AARPYLDLKA LERALVETRA DAAWVGWGFV AEDPAFAELC ERVGVTFVGP SPEAMRKLGD
KIGAKLIAEE VGVPVAPWSR GAVDTLDAAL AAATEIGYPL MLKATAGGGG RGIRVITNAA
ELADAYERTI QEAARAFGSG VVFLERLVTG ARHVEVQVIA DGQGTAWALG VRDCSVQRRN
QKIIEESSSP VLGPEQVAEL KASAERLAVA VGYRGAATVE FLYHPGDRLF AFLEVNTRLQ
VEHPITELTT GFDLVKAQLH VASGGRLDGR PPVERGHAVE ARLNAEDPDR DFAPSPGRIA
RLDLPAGPGI RVDTGVSEGD TIPGDFDSMI AKIIAYGRDR HEALGRLRRA MAETTVIIDG
GATNKSFVLD LLDQPEVIDA SADTGWIDRV RGEGRLVSHR HSAVALAAAA IEAYEEEERV
ERQRLLSTAF GGRPQVQHSS GRPLDLKLRG IGYRVRVARI GAHRFRVGIE VGGDVRTADV
ELDRFDRHTG QIVVNGTRYR LLTGTHGPVH LVEVDGVTHR VSRDEGGVIR SSMPALVVAT
PLEVGAEVEA GAPVLVLESM KMETVLRAPF KARLKECVVS VGSQVETGAP LLRLEPLADD
AAEDTSATEA VELDLPVAPG DAPVRSRTRR GQEDLRSLLL GFDVDPHDDR RVLDDYLVAR
QVATAQGYRP LAGEIDLIDM FADLAELSRN RPTGEDGGDG SHVHSAREYF HTYLQSLDVE
RAGLPETFQA KLATALGHYG VTELDRSPDL EAAVFRIFLA LQRASADAAV VATLLRAWLR
EAPPDETLRE PAGLALERLV AATQVRFPVV SDLARGVVFA WFGQPLLRRN RARVYAGVRR
HLRHLDAHPD APDRAERIAE MVRSTEPLVR LLGQRLGRAD LDNVVMLEVL TRRYYGNKGL
TAVRTREVSG CTFVVAERAD SSVVSCAVGF DALGSALRGL AELADGEAAI DADIYLAWEN
QPADSEAMAT ALHEVVSAHP LPHPVRRLTL AVAGRSGAVM HHHFTFRPST TGMTEERLIR
GLHPYIAQRM QLERLSKFDL TRLPSADEEV YLFQCVAREN PSDDRLVAFA QVRDLTALRE
HDGRLVALPT AEDTLATCLD SIRRAQARRP SKKRFTTNRI VLYVWPPSDL TRAELETIAA
RVLPTTAGAG LEEILFIARQ RDPETGELTK IAVRISIDAA GGTELTVGEP SDEPIEPLDD
YRQKVLRASS RNTVYPYELT TALGDFVEHD LDDTHTLVPV DRPKGRNRAA IVAGVLSTPT
RRHPEGVTRV VLLGDPTKSL GALSEPECRR VVAALDLAER MRVPLEWWAL SAGARISMES
GTENMDWVAA ALKRIVEFTQ AGGEINIVVA GITVGAQPYW NAEATMLMHT RGILVMTPDS
AMVLTGKQSL DFSGGVSAED NFGIGGYDRV MGPNGQAQYW APNLAAARDV LMSYYDHTYV
VPGEESPRRV PTTDPVDRDV SDFPHVVAGS DFTTVGEIFS ATANPDRKKP FDIRTVMRAL
SDQDHPVLER WAGMADAETV SVQDVHLGGT PVCLIGIESR AVPRRGFPPT DGPDTYTAGT
LFPQSSKKAA RAINAASGNR PLVVLANLSG FDGSPESMRK LQLEYGAEIG RAIVNFRGPI
VFCVISRYHG GAFVVFSKAL NPNMTVLALE GSFASVLGGA PAAAVVFSGD VNARTAADPR
VRDLEARVAA ATGADRAALT AELDELRLSV RAEKLGEVAT EFDRVHNIHR AVEVGSVDAV
IRAAELRPRI IEAIGSRRG
//
