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};
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; 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
//