ID A9M6M3_BRUC2 Unreviewed; 673 AA.
AC A9M6M3;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:ABX61124.1};
GN OrderedLocusNames=BCAN_A0018 {ECO:0000313|EMBL:ABX61124.1};
OS Brucella canis (strain ATCC 23365 / NCTC 10854).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=483179 {ECO:0000313|EMBL:ABX61124.1, ECO:0000313|Proteomes:UP000001385};
RN [1] {ECO:0000313|EMBL:ABX61124.1, ECO:0000313|Proteomes:UP000001385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23365 / NCTC 10854 {ECO:0000313|Proteomes:UP000001385};
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP000872; ABX61124.1; -; Genomic_DNA.
DR RefSeq; WP_006133047.1; NC_010103.1.
DR AlphaFoldDB; A9M6M3; -.
DR GeneID; 55589823; -.
DR KEGG; bcs:BCAN_A0018; -.
DR HOGENOM; CLU_000395_3_1_5; -.
DR PhylomeDB; A9M6M3; -.
DR Proteomes; UP000001385; Chromosome I.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
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 19..467
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 138..340
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 592..669
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 673 AA; 72316 MW; 787FDFA8CBF5C375 CRC64;
MRKSVKRFSA RIPRGKNAMF QKILIANRGE IACRVIRTAC KLGIATVAIY SDADARALHV
EMADEAVRVG PAASAQSYLN VDAIIKAAKE TGAEAIHPGY GFLSENPAFV DAVEEAGLIF
IGPSAKAIRA MGLKDAAKAL MEKAGVPVVP GYHGDNQDGA FLKSEADRIT YPVLIKARAG
GGGKGMCRVD SAADFAAALE SARREAEASF GDGAVLVEKY MAKPRHIEVQ VFGDNHGNAV
HLFERDCSLQ RRHQKVIEEA PAPGMTEEMR AAMGEAAVKA ALTIGYSGAG TVEFIADVSE
GLRPDRFFFM EMNTRLQVEH PVTEAITGRD LVEWQLRVAS GEALPKRQDE LSINGWAFEA
RLYAEDPARD FLPATGKLAL FVPPENARVD SGVRTGDTIT PFYDPMIAKI ITHGATRDEA
LNRLDAALNK TRIAGLVTNR QFLSALCNLE AFRTGDVDTG LIGRETAALF TDAQPSDIAF
ALAALGALDL LDAPEKSDPW SGLRGFRLWG EASRSVLIEH HGERRTVSFT ARGDRHFGFA
FGTMDIRAHK NGLVRFAIDG RVSEASVSRI GHDVTVQIEG HDTIFHHVLA TGAEEDASSE
SRILSPMPGL VRLVSVVEGA SVAKGDPLVT MEAMKMELSL TAPRDGKVAS VTVAAGDQVN
EGALLVELEE QHG
//
