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Database: UniProt
Entry: A0A2K5ZRP9_MANLE
LinkDB: A0A2K5ZRP9_MANLE
Original site: A0A2K5ZRP9_MANLE 
ID   A0A2K5ZRP9_MANLE        Unreviewed;       434 AA.
AC   A0A2K5ZRP9;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Methylcrotonyl-CoA carboxylase subunit 1 {ECO:0000313|Ensembl:ENSMLEP00000030492.1};
GN   Name=MCCC1 {ECO:0000313|Ensembl:ENSMLEP00000030492.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000030492.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000030492.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A2K5ZRP9; -.
DR   Ensembl; ENSMLET00000054057.1; ENSMLEP00000030492.1; ENSMLEG00000039351.1.
DR   GeneTree; ENSGT00940000156941; -.
DR   Proteomes; UP000233140; Unplaced.
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   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_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; 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   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 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   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT   DOMAIN          10..434
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          129..326
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   434 AA;  48161 MW;  1C566884AB30AF3A CRC64;
     MKYTTTTGRN ITKVLIANRG EIACRVMRTA RKLGVQSVAV YSEADRNSMH VDMADEAYSI
     GPAPSQQSYL SMEKIIQVAK TSAAQAIHPG YGFLSENMEF AELCKQEGII FIGPSPSAIR
     DMGIKSTSKS IMAAAGVPVV EGYHGEDQSD QCLKEHAGRI GYPVMIKAVR GGGGKGMRIV
     RSEQEFQEQL ESARREAKKS FSDDAVLIEK FVDTPRHVEV QVFGDHHGNA VYLFERDCSV
     QRRHQKIIEE APAPGIKPEV RKKLGEAAVR AAKAVNYVGA GTVEFIMDSK HNFYFMEMNT
     RLQVEHPVTE MITGTDLVEW QLRIAAGEKI PLSQEEITLQ GHAFEARIYA EDPSNNFMPG
     AGPLVHLSTP RADPSTRIET GVRQGDEVSV HYDPMIAKLV VWAADRQAAL TKLRYSLRQY
     NINSLHFHLA VEED
//
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