ID A0A014NYY1_9BURK Unreviewed; 578 AA.
AC A0A014NYY1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:EXU79115.1};
GN ORFNames=AX13_07900 {ECO:0000313|EMBL:EXU79115.1};
OS Comamonas aquatica DA1877.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=1457173 {ECO:0000313|EMBL:EXU79115.1, ECO:0000313|Proteomes:UP000020766};
RN [1] {ECO:0000313|EMBL:EXU79115.1, ECO:0000313|Proteomes:UP000020766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA1877 {ECO:0000313|EMBL:EXU79115.1,
RC ECO:0000313|Proteomes:UP000020766};
RA Watson E., Macneil L.T., Ritter A.D., Yilmaz L.S., Rosebrock A.P.,
RA Caudy A.A., Walhout A.J.;
RT "Interspecies Systems Biology Uncovers Metabolites Affecting C. elegans
RT Gene Expression and Life History Traits.";
RL Submitted (JAN-2014) 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:EXU79115.1}.
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; JBOK01000020; EXU79115.1; -; Genomic_DNA.
DR RefSeq; WP_043386203.1; NZ_JBOK01000020.1.
DR AlphaFoldDB; A0A014NYY1; -.
DR STRING; 225991.MA05_08510; -.
DR PATRIC; fig|1457173.3.peg.3003; -.
DR Proteomes; UP000020766; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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; 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; 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; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
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; PS00867; CPSASE_2; 1.
PE 4: Predicted;
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000020766}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 500..575
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 578 AA; 61314 MW; DFFB7E169A17F14B CRC64;
MRKVLIANRG EIAVRIARAC RDYGVQSVAV YADPDADALH VRMADEAWGL DGVRPAQTYL
DMDKLIAVAR KSGADAVHPG YGFLSERAEF ARAVIDAGLT WIGPRPETIE ALGDKVAARK
IALQVGAPLV AGTADPVQSA AEVQAFAQQH GLPVAIKAAF GGGGRGLKVA WQMDEVAELF
ESAVREATAA FGRGECFLEQ FLDRPRHIEA QVLGDQHGNV VVVGTRDCSL QRRNQKLVEE
APAPFLTEAQ RASIHQAARD ICAAAGYVSA GTVEFLLSRS GQISFLEVNT RLQVEHPVTE
ETTGIDLVLE QLRIADGLPL SFSQTPTPRG HSIEFRINAE DPGRGYLPTP GLIQRFEAPS
GGGVRVDSGV MSGSTVPGSF DSMMAKLIVT GATREQALAR ARRALQEFTI EGVASVLPFH
RAVVQDPAFT AEQGFQVHTR WIETEMAQTW VEAARPGAPV DQPLQRCFIE LEGKRVALGL
PASLLQAWGS VSSAASPAAA PQAEASADAI TAPMAGSLVQ WKLADGAAVQ AGDVVAVMES
MKMESPITAP QAGRLQQQVA PGAVLQAGQV IARVVAGQ
//
