ID I8T2I7_9GAMM Unreviewed; 497 AA.
AC I8T2I7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Acetyl/propionyl CoA carboxylase alpha subunit {ECO:0000313|EMBL:EIT67888.1};
GN ORFNames=WQQ_43230 {ECO:0000313|EMBL:EIT67888.1};
OS Hydrocarboniphaga effusa AP103.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Hydrocarboniphaga.
OX NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT67888.1, ECO:0000313|Proteomes:UP000003704};
RN [1] {ECO:0000313|EMBL:EIT67888.1, ECO:0000313|Proteomes:UP000003704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP103 {ECO:0000313|EMBL:EIT67888.1,
RC ECO:0000313|Proteomes:UP000003704};
RX PubMed=22933753; DOI=10.1128/JB.01017-12;
RA Chang H.K., Zylstra G.J., Chae J.C.;
RT "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain
RT AP103T (ATCC BAA-332T).";
RL J. Bacteriol. 194:5120-5120(2012).
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:EIT67888.1}.
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DR EMBL; AKGD01000004; EIT67888.1; -; Genomic_DNA.
DR RefSeq; WP_007187258.1; NZ_AKGD01000004.1.
DR AlphaFoldDB; I8T2I7; -.
DR STRING; 1172194.WQQ_43230; -.
DR PATRIC; fig|1172194.4.peg.4189; -.
DR Proteomes; UP000003704; 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 Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_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; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000003704}.
FT DOMAIN 8..452
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 127..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 497 AA; 53647 MW; 98453E0CD3709F8E CRC64;
MSKTNAWPFK SVLIANRGEI AVRVLRTVQQ LGLRGIVVYH AADRGAPAVK LADEAIEITG
STPVAAYLDA AQILEAARRS DAGAIHPGYG FLSENKAFAS AVEAAGIVFI GPKPEHIDLM
GDKVRARNFV QKAGFPVAPS AIEDDDPASF VERARKVGAP LLIKPSAGGG GKGMRIVRDL
SLLEAEIERA RSEGQRYFGD GRLYVERYIE NPRHIEVQVL GDSHGNVVHV FERECSVQRR
FQKIVEETPS PALTQELRMS ICETAAGIAR SAGYRNAGTV EFIFGQDGEF FFLEMNTRLQ
VEHPVTEEIT GLDLVHEQLR IAAGEPLGYP QREVTTQGHA IEFRIYAEDA GRGYTPTTGP
ILLLRPPQGE GVRWDSGVTQ GGEVTSAFDP MIAKLIVHGA DRNEAIARAD AALRDTVLLG
CKTNTAFLRR LVAHPAFVAG DVHTGFLDAN PQIAAEPEIA NDSLQALLAT AALSTRPMID
AADAIPDLHA AIGSWTN
//
