ID C4RBB4_MICS3 Unreviewed; 1850 AA.
AC C4RBB4;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Acetyl/propionyl-CoA carboxylase alpha subunit {ECO:0000313|EMBL:EEP69677.1};
GN ORFNames=MCAG_00004 {ECO:0000313|EMBL:EEP69677.1};
OS Micromonospora sp. (strain ATCC 39149 / NRRL 15099 / SCC 1413).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=219305 {ECO:0000313|EMBL:EEP69677.1, ECO:0000313|Proteomes:UP000010307};
RN [1] {ECO:0000313|Proteomes:UP000010307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39149 / NRRL 15099 / SCC 1413
RC {ECO:0000313|Proteomes:UP000010307};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Galagan J., Nusbaum C., Birren B.;
RT "The genome sequence of Micromonospora carbonacea var. africana strain ATCC
RT 39149.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; GG657738; EEP69677.1; -; Genomic_DNA.
DR STRING; 219305.MCAG_00004; -.
DR eggNOG; COG4770; Bacteria.
DR eggNOG; COG4799; Bacteria.
DR HOGENOM; CLU_239133_0_0_11; -.
DR Proteomes; UP000010307; 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:UP000010307}.
FT DOMAIN 34..484
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 158..355
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 604..687
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1568..1850
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1534..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1850 AA; 200536 MW; AFA6E2207AA10D97 CRC64;
MRHGAARRYT EGWALPGPQC RARPSSVYRR AGSVFSRVAI VNRGEAAMRL IHAVRDLAAE
TGTRIETVAL HTDVDRAATF VREADLTYDL GPASARPYLD LKALERALVE TGADAAWVGW
GFVAEDPAFA ELCERVGVTF VGPSADAMRK LGDKIGAKLI AEEVGVPVAP WSRGAVETLD
AALVAAAEIG YPLMLKATAG GGGRGIRVVS NSDELADAYE RTSQEAARAF GSGVVFLERL
VTGARHVEVQ VIADGVTAWA LGVRDCSVQR RNQKVIEESA SPVLSAAQAA ELKASAERLA
VAVGYRGAAT VEFLYHPGDR LFAFLEVNTR LQVEHPITEV TCGFDLVKAQ LHVASGGRLD
GEPPAERGHA VEARLNAEDP DRDFAPSPGR IARLDLPAGP GIRVDTGVSE GDTIPADFDS
MIAKIIAYGR DRDEALGRLR RAMAETTVII EGGATNKSFV LDLLDQPEVI DASADTGWID
RVRGEGRLVT HRHSAVALAA AAIEAYEEEE RVERQRLLST AFGGRPQVQH ASGRPLDLKL
RGVGYRVRVA RVGAHRFRVG IEAGDGVRTA DVELDRFDRH TGQIVVNGAR YRLLTGTHGP
VHLVEVDGVT HRVSRDEGGV VRSPAPALVV ATPLEVGAEV EAGAPVLVLE SMKMETVLRA
PFRARLKECA VSVGSQVETG APLLRLEPLA DDTEAEDTSA AGAVELDLPA APAPIPPRER
TTRGQEDLRS LLLGFDVDPH DDRRVLDGYL AARRAATEDG YRPLAEELGL VDVFADLAEL
SRNRPAGEDG DGHVFSAREY FHTYLQCLDV ERAGLPETFQ AKLAKALGHY GVTELERTPA
LEAAVFRIFL ALQRASADAT VIATLLREWL REPPPDEVLR EPAGLALERL VAATQVRFPV
VADLARGVVF AWLGQPLLRR NRARVYAAVR RHLRHLDAHP DAPDRAERVA EMVRSTEPLV
RLLGQRLVRD HLDNAVMLEV LTRRYYGNKG LTGVRTSEVA GCTFVVAERA DSRVVSAAVR
FEALGDALRG LAELAGGEDA VDADIYLAWE RQPEDSEAMA AALHEVVGAY PLPNQVRRIT
ATVAGRSGAV MHHHFTFRPS TAGMVEERLV RFLHPYIAQR MQLERLRKFD LTRLPSSDEE
VYLFRCVARE NPSDERLVAF AQVRDLTELR EHDGRLVALP TAEDTVAACL DSIRRAQSRR
PSSKRVNTNR IVVYVWPPSD ITRAELETIA GRVLPTTAGA GLEEILFIAR QHDRDTGELT
KIAVRVSFDA TGGWELTVGE PSDEPVEPLD EYRQKVLRAA SRNTVYPYEL TALLGEFVEH
DLDERHALVP VDRPRGRNTA AIVAGVVTTR TARYPEGVTR VVLLGDPTKS LGALSEPECR
RVIAALDLAE RMRVPLEWYA LSSGARISME SGTENMDWVA AALKRIVEFT QDGGEINIVV
AGINVGAQPY WNAEATMLMH TKGVLVMTPD SAMVLTGKQS LDFSGGVSAE DNFGIGGYDR
VMGPNGQAQY WAPNLTAARD VLMAHYDHTY VAPGESAPRR ATTTDPVDRD ISDFPHVMAG
SDFTTVGEIF SAEANPDRKK PFDIRSVMRA LSDQDHPVLE RWAGMADAET AVVQDVHLGG
MPVCLLGIES RSVPRRGFPP TDGPDTYTAG TLFPRSSKKA ARAINAASGN RPLVVLANLS
GFDGSPESMR KLQLEYGAEI GRAIVNFRGP IVFCVISRYH GGAFVVFSKA LNPNMTVLAL
EGSFASVLGG APAAAVVFSG DVNARTAADP RVRDLEARVA AASGTDRAAL TAELDELRSS
VRAEKLGEVA AEFDRVHNIQ RAVEVGSVDA VIRAAELRPR IIEAIESGAR
//
