ID A0A3Q0SZ29_AMPCI Unreviewed; 548 AA.
AC A0A3Q0SZ29;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase 1 (alpha) {ECO:0000313|Ensembl:ENSACIP00000030131.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000030131.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000030131.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3Q0SZ29; -.
DR Ensembl; ENSACIT00000030923.1; ENSACIP00000030131.1; ENSACIG00000023146.1.
DR GeneTree; ENSGT00940000156941; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 3.30.700.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
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; 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; 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; 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; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 1..341
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 14..211
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 456..536
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 548 AA; 59972 MW; 4C491B6CB295B5ED CRC64;
MEKVLEVAKK SGSHHIMSAA GVPIIGGYHG EDQSNENLQA EAARIGYPVM IKAVRGGGGK
GMRIARSDSD FLEQLESARR EARKSFNDDV MLIEKFVEDP RHVEVQVFGD MHGNAVYLFE
RDCSVQRRHQ KIIEEAPGPG ISPEVRRKLG EAAVRAAKAV NYVGAGTVEF IMDAEHNFYF
MEMNTRLQVE HPVSEMITGT DLVEWQLRVA AGERLPLLQD DIILRGHSFE ARIYAEDPNN
DFLPGAGPLL HLSTPPPDQH TRIETGVREG DEVSAHYDPM IAKLVVWGED RSAALKKLRY
SLRQYNIVGL NTNIDFLLSL SGHPEFEAGN VSTSFIPQHY ADLFPTPKAP SGATICQAAL
GLVLQERIHT RGFTQSSTDP FSPFGSSSGW RNNILFNRNV TLQLGDKREV ETEGGASFLH
CTVNGVKSRP KLVILDNTVH LFSTEGSSEV SVPVPKYRAG VSGSGAQGGA VAPMTGTIEK
VLVKAGDKVT VGDPLMVMIA MKMEHTIRAP KSGVIKKVFF SEGSQANRHA PLVELVEEEE
EVGEGSSQ
//
