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Database: UniProt
Entry: H6R8U3_NOCCG
LinkDB: H6R8U3_NOCCG
Original site: H6R8U3_NOCCG 
ID   H6R8U3_NOCCG            Unreviewed;      1820 AA.
AC   H6R8U3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Putative Acetyl/propionyl-CoA carboxylase alpha subunit {ECO:0000313|EMBL:CCF62317.1};
GN   OrderedLocusNames=NOCYR_1522 {ECO:0000313|EMBL:CCF62317.1};
OS   Nocardia cyriacigeorgica (strain GUH-2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF62317.1, ECO:0000313|Proteomes:UP000008190};
RN   [1] {ECO:0000313|EMBL:CCF62317.1, ECO:0000313|Proteomes:UP000008190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GUH-2 {ECO:0000313|EMBL:CCF62317.1,
RC   ECO:0000313|Proteomes:UP000008190};
RX   PubMed=22461543; DOI=10.1128/JB.00161-12;
RA   Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L.,
RA   Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S.,
RA   Nazaret S., Neto M., Petit S., Roche D., Vallenet D., Rodriguez-Nava V.,
RA   Richard Y., Cournoyer B., Blaha D.;
RT   "Genome sequence of the human- and animal-pathogenic strain Nocardia
RT   cyriacigeorgica GUH-2.";
RL   J. Bacteriol. 194:2098-2099(2012).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; FO082843; CCF62317.1; -; Genomic_DNA.
DR   RefSeq; WP_014349784.1; NC_016887.1.
DR   STRING; 1127134.NOCYR_1522; -.
DR   KEGG; ncy:NOCYR_1522; -.
DR   eggNOG; COG4770; Bacteria.
DR   eggNOG; COG4799; Bacteria.
DR   HOGENOM; CLU_239133_0_0_11; -.
DR   OMA; NTVYPYE; -.
DR   OrthoDB; 4435847at2; -.
DR   Proteomes; UP000008190; Chromosome.
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 CARBOXYL CARRIER PROTEIN; 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:UP000008190}.
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..1816
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   1820 AA;  197486 MW;  A18D75694F3EAA85 CRC64;
     MFSRIAIVNR GEAAMRLIHA VRDLAAATAQ QIETVALYTD VDRTATFVRE ADIAYDLGPA
     SARPYLDLKA LERALRATKA DAAWVGWGFV AEDPAFAELC EQIGVTFIGP SPDAMRKLGD
     KIGAKLIAEE VGVPVAPWSR GAVESVEAAV AAAAEIGYPL MLKATAGGGG RGIRKINDEA
     ELVDAYERTS QEAARAFGSG VVFLERLVTG ARHVEVQVIA DGQGTAWALG VRDCSVQRRN
     QKIIEESASP VLSPQQAADL KASAERLAVA VGYRGAATVE FLYHPGDQLF AFLEVNTRLQ
     VEHPITEYTT GFDLVHAQLH VASGGRLEGE PPAERGHAIE ARLNAEDPDR DFAPAPGRIA
     LLDLPAGPGI RVDTGVSEGD TIPADFDSMI AKIIAYGRNR EEALGRLRRA VSQTRVIIEG
     GATNKSFVLD LLDQPEVIDA SADTGWIDRV RGEGRLVSQR HSAVALAAAA IEAYEEEERV
     ERHRLLSTAS GGRPQVQHES GRPLDLKLRG VGYRVRVARI GAHRFRIGIE AGTEIRTADV
     DLERFDQHTG QIVVNGIRYR VVTGTHGPVH LVDVDGVTHR VSRDEGGVVR SPAPALVVAT
     PLQVGDEVEA GAPVLVLESM KMETVLRAPF RARLKECSVS VGTQVEAGAP MLRLEPLADD
     AEAADTGANE PVELDLPAAP ARTQPHELLA RGQQDMRSLL LGFDVDPHDD RRVIEDYLAA
     RREAIADNRR PLAEELELIE VFADLAELSH NRTWGDDGGQ AHVHSAREYF HTYLQSLDVD
     RAGLPESYQA KLARALGHYG VTELDRTPEL EAAVFRIFLA QQRPSDTVMV VTTLLREWLS
     EPVPDAALRE PVGLALERLV AATQVRFPVI ADLTRGLVYA WYGQPLLRRN RARVYANVRK
     HLSYLDANPA APDRAERLAE MVRSTEPLVR LLGQRLERGS ADNTVMLEVL TRRYYGNKDL
     VDVRTQQAGG CTFVVAERRG LTLVSAAVSF DDLGSVVAGL AELAGGAASI EADIYLSWEG
     QPEDFDEMAA ALQEVLSAQP LPNQVHRITA TVAGSGGAVM HHHFTYRPSA TGMDEERLIR
     GLHPYIAERM QLKRLRKFDL TRLPSSDEEV YLFRCVAKEN SSDERLIAFT QVRDLAALRE
     HDGRLLALPT AESTLAACVD GIRRAQSLRG SGNRLHTNRI VMYIWPPLDL TEAELSTIVE
     RVEPSTGGAG LEEILLIARR PDPETGELVK IVVRIGFDAP GWTQVTVGER TDDPVEPIDE
     YRQKVLRAVS RNTVYPYELT GLLGDFTEYD LDDNHALVPV DRPKGRNRAA IVAGVVTAPT
     ERHPQGVTRV VLLGDPTKSL GALSEPECRR VIAALDLAEQ MQVPLEWYAL SSGARISMTS
     GTENMDWVAA ALKRIVEFTQ DGGEINIVVA GINVGAQPYW NAEATMLMHT KGILVMTPDS
     AMVLTGKQAL DFSGGVSAED NFGIGGYDRV MGPNGQAQYW APNLAAAQEI LMSHYDHTYI
     APGEQAPRRA QTSDPIDRDV TGYPHVMADS DFTTVGEIFS ATANPDRKKP FDIRTVMRAL
     SDQDHPVLER WAGMADAETA VVQDAHLGGI PVCLLGIESR GIPRRGFPST DGPDTYTAGT
     LFPRSSKKAA RAINAASGNR PLVVLANLSG FDGSPESMRK LQLEYGAEIG RAIVNFQGPI
     VFCVISRYHG GAFVVFSKAL NPNMTVLALE GSFASVLGGA PAAAAVFSGE VNARTAADPR
     IQDLETRAAN ASGTDRAELT AELDELRSSV RAEKLGDVAA EFDKVHNIHR AVEVGSVDAV
     IRAAELRPRI IEAIEARLGN
//
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