ID A0A2D0RTX9_ICTPU Unreviewed; 711 AA.
AC A0A2D0RTX9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0000313|RefSeq:XP_017333420.1, ECO:0000313|RefSeq:XP_053539171.1};
GN Name=mccc1 {ECO:0000313|RefSeq:XP_017333420.1,
GN ECO:0000313|RefSeq:XP_053539171.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017333420.1};
RN [1] {ECO:0000313|RefSeq:XP_017333420.1, ECO:0000313|RefSeq:XP_053539171.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017333420.1,
RC ECO:0000313|RefSeq:XP_053539171.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR RefSeq; XP_017333420.1; XM_017477931.3.
DR RefSeq; XP_053539171.1; XM_053683196.1.
DR STRING; 7998.ENSIPUP00000036747; -.
DR Ensembl; ENSIPUT00000038183; ENSIPUP00000036747; ENSIPUG00000024615.
DR GeneID; 108270914; -.
DR KEGG; ipu:108270914; -.
DR CTD; 56922; -.
DR OMA; FINKPKH; -.
DR OrthoDB; 1129179at2759; -.
DR Proteomes; UP000221080; Chromosome 10.
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; 3.30.700.40; -; 1.
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; 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; 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; PS00188; BIOTIN; 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 Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 35..481
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 154..351
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 624..702
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 711 AA; 78183 MW; 448E39A0F57DDF61 CRC64;
MAAAVLQVRV NQTLRAQLQK LIWSRGAVRH ASVGRIEKVL IANRGEIACR VMRTAKKMGV
RSVAVYSDAD RHSMHVAMAD EAYHIGAAPS QQSYLCMEKV LEIAKKSSAQ AVHPGYGFLS
ENTEFAELCK QEGIIFIGPP SSAIRDMGIK STSKYIMSAA GVPIIEGYHG EDQSDEKLQA
EAARIGYPVM IKAVRGGGGK GMRIARSEAE FHEQLESARR EALKSFNDDV MLVEKFVDNP
RHVEVQVFGD QHGNAVYLFE RDCSVQRRHQ KIIEEAPGPG ISPEVRRKLG EAAVRAAKAV
NYVGAGTVEF IMDSQHNFYF MEMNTRLQVE HPVSEMITGT DLVEWQLRVA AGEKLPLSQD
EIVLQGHSFE ARIYAEDPNN DFLPGAGPLL HLSTPQEETQ TRIETGVRQG DEVSVHYDPM
IAKLVVWGED RSAALKKLRY CLRQYNIVGL NTNIDFLLSL SGHAEFEAGN VHTSFIQQHY
DQLFPKPTAP GGDIVCQAAL GLLLQEREHT LEFLHQSHDV FSPFGSGNGS RLNVLYCRNL
TLQLGENKVT VAVTYNPDGT YRMEAGGQVF QVSGELQKVG GATYLHSCVN GVLSRPKLVI
LDNTVHLFSM EGSVEVKVPL PKFLAGVSSS GAQDGAVAPM TGTIEKVLVK VGDAVQKGDP
LMVMIAMKME HTIRAPKAGV IKRVLFKEGS QASRHAALVE MEEEQEEEAQ S
//
