ID A0A1D8TCG7_9NOCA Unreviewed; 1051 AA.
AC A0A1D8TCG7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Carbamoyl-phosphate-synthetase {ECO:0000313|EMBL:AOW95269.1};
GN ORFNames=BFN03_19385 {ECO:0000313|EMBL:AOW95269.1};
OS Rhodococcus sp. WMMA185.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=679318 {ECO:0000313|EMBL:AOW95269.1, ECO:0000313|Proteomes:UP000178767};
RN [1] {ECO:0000313|EMBL:AOW95269.1, ECO:0000313|Proteomes:UP000178767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMMA185 {ECO:0000313|EMBL:AOW95269.1,
RC ECO:0000313|Proteomes:UP000178767};
RA Bugni T.S., Adnani N., Braun D., Chevrette M., McDonald B., Rajski S.;
RT "Draft Genome of Rhodococcus sp. WMMA185.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC {ECO:0000256|ARBA:ARBA00006102}.
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DR EMBL; CP017014; AOW95269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D8TCG7; -.
DR STRING; 679318.BFN03_19385; -.
DR KEGG; rhw:BFN03_19385; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000178767; Chromosome.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR011762; COA_CT_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 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; PS50980; COA_CT_NTER; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000178767}.
FT DOMAIN 1..441
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 96..294
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 457..534
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 541..819
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 813..1051
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1051 AA; 110982 MW; 43EF755C4F6BD486 CRC64;
MSVDTIALYA EDDADSPHVR AATEAVALNG SGPSTYLDAR AILDAADEFG ATMIHPGYGF
LSENADFARS CAAAGLTFVG PEPEILDIFG DKSLARKAAM SAKVPVLDAT PGPTDVDGVR
SFFSSHPQGI MLKALAGGGG RGIRAVHSAD RIEESYRLCA SEAQLGFGNP TLFAEALMPA
ARHIEVQVVA APDAGNIRAL AVGDRDCSVQ RRHQKLIETA PAQGLDAQLR TELHEAATRL
CSSIGYRGIA TVEFLVSPSG FVFLEVNPRI QVEHTVTEEV TGIDLVAAQI DISRGACFDE
LSLPEGISAV GLDTVGSAAT ARGIAIQARV NMETMRPDGQ AIPATGTLST FSAPNGPGVR
VDTYGRPGLS PSPRYDSLLA KVVVHSRSES FPAAVRKTVS ALSEFAIDGV PTNIGFLQAI
LADSDFPNGI VTTDFLDERM NTLADAAHSH SPAAASPGTL ELRTGEEVLR AHMAGTIVES
VGEGADVGTG GQLIVLEAMK MQHVISAPAE SVVERTLVSP GETVNAGDPL IVIRRTGPDA
DGIALSAIDL DRERQDLAEI RHRHEVTLDA ARPAAMAKRE KIGRRSARAN IGDLVDPGTF
VEYGPLVLAA QRSRRSEQDL IEKTPADGLI AGLANINGEV FGPSVSQAVV MSYDYSVLAG
TQGRNNHAKS DRMLEIAARK QIPVVLFAEG GGGRPGDTDA GPVSGLDLET FRSMAALNGK
VPLVSIVSGR CFAGNAALAG VCDVLIATPE ANIGMGGPAM VEGGGLGVYR PEEIGPVEVQ
RRNGVIDLLA RDEAHAVTLA KKYLSYFQGH VSDWIAPDER LSRHVVPENR LRAYDVRRAI
DAIADVDSAL ELRRDHGVGI VTALIRVEGR PYGLVANSSD HLGGAIDAVA ADKMAHFLEL
CESFGLPVVS LCDTPGFMVG PDSEKEATVR RFGKLFVAGA RMTVPYGTII LRKGYGLGAM
AMAGGSFHAS DFTVAWPTGE IGAMGLEGAV RLGFRKELEA IDDPDERQTA FNQLVDSAYE
HGKAINAATI FELDDVIDPA DSRTWIRRLH P
//
