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Database: UniProt
Entry: C4INL1_BRUAO
LinkDB: C4INL1_BRUAO
Original site: C4INL1_BRUAO 
ID   C4INL1_BRUAO            Unreviewed;       678 AA.
AC   C4INL1;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Acetyl-CoA carboxylase alpha chain / propionyl-CoA carboxylase alpha chain {ECO:0000313|EMBL:EEP63544.1};
GN   ORFNames=BAAA_1000016 {ECO:0000313|EMBL:EEP63544.1};
OS   Brucella abortus str. 2308 A.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=641140 {ECO:0000313|EMBL:EEP63544.1, ECO:0000313|Proteomes:UP000003313};
RN   [1] {ECO:0000313|EMBL:EEP63544.1, ECO:0000313|Proteomes:UP000003313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308 A {ECO:0000313|EMBL:EEP63544.1,
RC   ECO:0000313|Proteomes:UP000003313};
RA   Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA   Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA   Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA   Green L., Rogers Y., Detter J.C., Bruce D., Brettin T.S.;
RL   Submitted (MAY-2009) 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:EEP63544.1}.
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DR   EMBL; ACOR01000001; EEP63544.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4INL1; -.
DR   Proteomes; UP000003313; 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   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.700.40; -; 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; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 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}.
FT   DOMAIN          24..472
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          143..345
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          597..674
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   678 AA;  73008 MW;  C1FC6B8FB62AACD5 CRC64;
     MRKRGMRKSV KRFSARIPRG KNAMFQKILI ANRGEIACRV IRTARKLGIA TVAIYSDADA
     RALHVEMADE AVRVGPAASA QSYLNVDAII KAAKETGAEA IHPGYGFLSE NPAFVDAVEE
     AGLIFIGPSA KAIRAMGLKD AAKALMEKAG VPVVPGYHGD NQDGAFLKSE ADRITYPVLI
     KARAGGGGKG MRRVDSAADF AAALESARRE AEASFGDGAV LVEKYMAKPR HIEVQVFGDN
     HGNAVHLFER DCSLQRRHQK VIEEAPAPGM TEEMRAAMGE AAVKAALTIG YSGAGTVEFI
     ADVSEGLRPD RFFFMEMNTR LQVEHPVTEA ITGLDLVEWQ LRVASGEALP KRQDELSING
     WAFEARLYAE DPARDFLPAT GKLALFVPPE NARVDSGVRT GDTITPFYDP MIAKIITHGA
     TRDEALNRLD AALNKTRIAG LVTNRQFLSA LCNLEAFRTG DVDTGLIGRE TAALFTDAQP
     SDIAFALAAL GALDLLDAPE KSDPWSGLRG FRLWGEASRS VLIEHHGERR TVSFTARGDR
     HFGFAFGTMD IRAHKNGLVR FAIDGRVSEA SVSRIGHDVT VQIEGHDTIF HHVLATGAEE
     DASSESRILS PMPGLVRLVS VVEGASVAKG DPLVTMEAMK MELSLTAPRD GKVASVTVAA
     GDQVNEGALL VELEEQHG
//
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