ID N1JA92_BLUG1 Unreviewed; 698 AA.
AC N1JA92;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 13-SEP-2023, entry version 43.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0008006|Google:ProtNLM};
GN ORFNames=BGHDH14_bgh05966 {ECO:0000313|EMBL:CCU77485.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU77485.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU77485.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU77485.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
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:CCU77485.1}.
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; CAUH01003743; CCU77485.1; -; Genomic_DNA.
DR AlphaFoldDB; N1JA92; -.
DR STRING; 546991.N1JA92; -.
DR EnsemblFungi; BLGH_05241-mRNA-1; BLGH_05241-mRNA-1; BLGH_05241.
DR eggNOG; KOG0238; Eukaryota.
DR HOGENOM; CLU_000395_3_1_1; -.
DR InParanoid; N1JA92; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000015441; 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; 3.30.470.20; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000015441}.
FT DOMAIN 27..475
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 143..341
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 621..690
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 698 AA; 77409 MW; 37C0D29E7A21A6E1 CRC64;
MAFRRNRTLT QAFNSQHPYV KTANVRTIRS VLIANRGEIA LRVGRTASRL GIRCSTVYTD
LDAKSQHALS SPFASNLGSP SAYLDGEKII AIAKQQNCDA LHPGYGFLSE NSDFARRCME
EGLLFIGPSW KAIQAMGNKS QSKIIMTEAN VPCIPGYHGP NQTPKVLLDE AVKIGFPVMI
KAVKGGGGKG MRIAGTKAEF LDKLESAKRE GISSFGDDAM LIEKFIANPR HIEVQIFGDS
YGNVVTMGER DCSLQRRHQK IIEESPAPNL PKHVRQGLWQ KAHAAALAVA YEGAGTVEFI
YDNDSQNFFF MEMNTRLQVE HPVTEALTGE DLVHWQFKVA AGQPLPLSQD EINQRIMSRG
WALEARIYAE DPMRNFMPAS GKLTHLKVPK TSDSVRVDAG FIQGDTITPD YDGMIAKLIV
TGSDRGLAMR KLHTALQEYE VVGVQTNIEF LKNVCKSNDF LQGIFDTGYI QKHHKELFAS
EGHVSEIFAQ AALGLMLKSP FGNESVPGGS TIGFCGAIQR QFKFNSLSDK DETVSVLVTP
SARHCFRVEV IFKNSVKLFE NVTCEPGKLS TLTSFFTHTR IDSTVIQEKD VVHVYQHGKQ
NRIEIVPPVW VNKVMGFEDL LNNVFAPIPC KILRVEVKEG DLVEKNQPLV VIESMKMETI
IRSPQKGVIT KLVHKEGDIC KAGTKLVLFA EVNLIMIK
//
