ID J3K8S3_COCIM Unreviewed; 711 AA.
AC J3K8S3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:EAS31247.3};
GN ORFNames=CIMG_06726 {ECO:0000313|EMBL:EAS31247.3};
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS31247.3, ECO:0000313|Proteomes:UP000001261};
RN [1] {ECO:0000313|Proteomes:UP000001261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2] {ECO:0000313|Proteomes:UP000001261}
RP GENOME REANNOTATION.
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; GG704912; EAS31247.3; -; Genomic_DNA.
DR RefSeq; XP_001242830.1; XM_001242829.2.
DR AlphaFoldDB; J3K8S3; -.
DR STRING; 246410.J3K8S3; -.
DR GeneID; 4561808; -.
DR KEGG; cim:CIMG_06726; -.
DR VEuPathDB; FungiDB:CIMG_06726; -.
DR InParanoid; J3K8S3; -.
DR OMA; FINKPKH; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000001261; 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:UP000001261}.
FT DOMAIN 42..490
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 158..356
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 628..704
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 711 AA; 77588 MW; F738CD6702042668 CRC64;
MSLHSFISRL PPASSLSRRA LLRSAARNSS SLSSTAGRDG TPLNSILIAN RGEIALRVGR
TAGQHGVRVT TLYTDPDASS QHALSSPFAF NLGETSAYLD GDRIIEIAKR EGCKGIHPGY
GFLSENAGFA QKCTQAGLVF IGPPWKAIEA MGDKSRSKEI MTAAGVPCVP GYHGSNQDPD
LLQKEADKIG YPVLIKAIKG GGGKGMRICS SRETFQDQLM SAKSESKNSF GDDQVLIEKY
ITTPRHIEVQ VFADKHGNCV ALGERDCSIQ RRHQKILEES PAPHLPQATR KDIWEKARAA
ALAVGYEGAG TVEFIFDNDT GEFYFMEMNT RLQVEHPVTE MVTGQDLVHW QLLVAEGAPL
PLTQEEIEAK IATSGHAIEA RIYAENPDQG FVPDSGRLIH VRTPKPTEDI RIDAGFVAGD
EVSSHYDPMI SKLIVRGANR TEALRSLAAA LEQYEVAGPM TNIEFIKRVC RSADFAAGEV
ETGYIEKHRE ELFRKEPIEP EVLAQATLAC YLDGSLTGPA GSAVGFSPAY QQRQFAFVQA
TAPGEPEGTP FDTQIEQTGP NNFNITVDGK TFTNVQRRVG TAQNVFTSFF PHTRLDTTVI
RDEDNVTVFQ RGKQYRLRIP RAKWMEKALG IKDVANSVIA PMPCKILRVT VAEGDTVEKD
QPLVVIESMK METVIRAPHN GIISKVVHKQ GDICKAGTPL VEFAGGDEAG K
//
