ID A0A0J8REM2_COCIT Unreviewed; 678 AA.
AC A0A0J8REM2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:KMU83382.1};
GN ORFNames=CIHG_01164 {ECO:0000313|EMBL:KMU83382.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU83382.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
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};
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; DS016982; KMU83382.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8REM2; -.
DR STRING; 396776.A0A0J8REM2; -.
DR VEuPathDB; FungiDB:CIHG_01164; -.
DR eggNOG; KOG0238; Eukaryota.
DR Proteomes; UP000054563; 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:UP000054563}.
FT DOMAIN 6..457
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 595..671
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 678 AA; 74317 MW; FAE20CBC8F0F0548 CRC64;
MLTSLPVSSP FDCVLGGETV RIKADFRIRR VGRTAGQHGV RVTTLYTDPD ASSQHALSSP
FAFNLGETSA YLDGDRIIEI AKREGCKGIH PGYGFVGTPL FYAGLVFIGP PWKAIEAMGD
KSRSKEIMTA AGVPCVPGYH GSNQDPDLLQ KEADKIGYPV LIKAIKGGGG KGMRICSSRE
TFQDQLMSAK SESKNSFGDD QVLIEKYITT PRHIEVQVFA DKHGNCVALG ERDCSIQRRH
QKILEESPAP HLPQATRKDI WEKARAAALA VGYEGAGTVE FIFDNDTGEF YFMEMNTRLQ
VEHPVTEMVT GQDLVHWQLL VAEGAPLPLT QEEIEAKIAT SGHAIEARIY AENPDQGFVP
DSGRLIHVRT PKPTEDIRID AGFVAGDEVS SHYDPMISKL IVRGANRTEA LRSLAAALEQ
YEVAGPMTNI EFIKRVCRSA DFAAGEVETG YIEKHREELF RKEPIEPEVL AQATLACYLD
GSLTGPAGSA VGFSPAYQQR QFAFVQATAP GEPEGTPFDT QIEQTGPNNF NITVDGKTFT
NVQRRVGTAQ NVFTSFFPHT RLDTTVIRDE DNVTVFQRGK QYRLRIPRAK WMEKALGIKD
VANSVIAPMP CKILRVTVAE GDTVEKDQPL VVIESMKMET VIRAPHNGII SKVVHKQGDI
CKAGTPLVEF AGGDEAGK
//
