ID A0A0N0E3S2_9PSED Unreviewed; 647 AA.
AC A0A0N0E3S2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=3-methylcrotonoyl-CoA carboxylase, alpha subunit {ECO:0000313|EMBL:KPA90430.1};
DE EC=6.4.1.4 {ECO:0000313|EMBL:KPA90430.1};
GN ORFNames=PF66_02490 {ECO:0000313|EMBL:KPA90430.1};
OS Pseudomonas fuscovaginae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=50340 {ECO:0000313|EMBL:KPA90430.1, ECO:0000313|Proteomes:UP000037931};
RN [1] {ECO:0000313|EMBL:KPA90430.1, ECO:0000313|Proteomes:UP000037931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRRI 6609 {ECO:0000313|EMBL:KPA90430.1,
RC ECO:0000313|Proteomes:UP000037931};
RX PubMed=26422147;
RA Quibod I.L., Grande G., Oreiro E.G., Borja F.N., Dossa G.S., Mauleon R.,
RA Cruz C.V., Oliva R.;
RT "Rice-Infecting Pseudomonas Genomes Are Highly Accessorized and Harbor
RT Multiple Putative Virulence Mechanisms to Cause Sheath Brown Rot.";
RL PLoS ONE 10:E0139256-E0139256(2015).
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:KPA90430.1}.
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DR EMBL; JSYZ01000009; KPA90430.1; -; Genomic_DNA.
DR RefSeq; WP_054062826.1; NZ_JSYZ01000009.1.
DR AlphaFoldDB; A0A0N0E3S2; -.
DR STRING; 50340.PF66_02490; -.
DR PATRIC; fig|50340.43.peg.5876; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000037931; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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; IPR048429; MCC_alpha_BT.
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 Pfam; PF21139; MCC_alpha_BT; 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; PS00866; CPSASE_1; 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, ECO:0000313|EMBL:KPA90430.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 5..451
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 124..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 568..647
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 647 AA; 69517 MW; 1B697825D846ED5D CRC64;
MSAPVITTLL VANRGEIACR VMRTAKAMGL TTVAVHSAID RDARHSREAD IRVDLGGSKA
AESYLRIDKL IAAAQASGAQ AIHPGYGFLS ENADFARAVE AAGLVLLGPP ATAIDAMGSK
SAAKALMETA GVPLVPGYHG EAQDLETFRE AAARIGYPVL LKATAGGGGK GMKVVEEPGQ
LAEALASAQR EAQSSFGDSR MLVEKYLLKP RHVEIQVFAD RHGNCLYLNE RDCSIQRRHQ
KVVEEAPAPG LSPALRQAMG EAAVRAAQAI GYVGAGTVEF LLDSRGEFFF MEMNTRLQVE
HPVTEAITGL DLVAWQIRVA SGEVLPISQQ DVPLLGHAIE VRLYAEDPGN DFLPATGRLE
VYRESAAGPG RRVDSGVAEG DSISPFYDPM LGKLIAWGES REQARLRLLA MLDEFAVGGL
KSNVAFLRRI IGHPAFAAAE LDTGFIPRYQ EQLLPPAEPL SDEFWQVAAR AWVLSLPETR
REDDPASPWS GRNGLRAGLP SEIVVHLSCR NEDRAVTLAE DLAITLQGET LSIEHQGVGQ
RHRLIRQGTE LYLQWQGELL AISAFDPIAA VEASHGHQGG LTAPMNGSIV RILVEVGQTV
EAGTQLVVLE AMKMEHSIRA PQAGVIKALY CQEGEMVAEG SALVELE
//
