ID A0A093G1V6_TYTAL Unreviewed; 699 AA.
AC A0A093G1V6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=N341_11668 {ECO:0000313|EMBL:KFV60609.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV60609.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV60609.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV60609.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; KK402416; KFV60609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093G1V6; -.
DR Proteomes; UP000054190; 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; 3.30.700.40; -; 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}; Reference proteome {ECO:0000313|Proteomes:UP000054190}.
FT DOMAIN 25..471
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 144..341
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 617..692
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV60609.1"
FT NON_TER 699
FT /evidence="ECO:0000313|EMBL:KFV60609.1"
SQ SEQUENCE 699 AA; 77700 MW; A839113CDECED7D6 CRC64;
CLQLYRQWNH VQRFVKWAST IGGHHIGKIL IANRGEIACR VMRTAKKMGV KSVAVYSEAD
RNSMHVAMAD EAYCIGPAPS QQSYLAMEKI MQVAKVSAAQ AIHPGYGFLS ENTEFAELCK
QEGIIFIGPP SSAIRDMGIK STSKAIMSAA GVPVVEGYHG EDQSDECLKE HAKRIGYPVM
IKAVRGGGGK GMRIAHSEKE FRDQLESARR EAKKSFNDDA MLIEKFVDNP RHVEVQVFGD
QHGNAVYLFE RDCSVQRRHQ KIIEEAPGPG INHEVRKRLG EAAVKAAKAV NYVGAGTVEF
IMDSRHNFYF MEMNTRLQVE HPVTEMITGT DLVEWQLRVA AGEKIPLRQE EILLRGHAFE
ARIYAEDPNN NFMPGAGPLL HLSTPPPDSF TRIETGVRQG DEVSVHYDPM IAKLVVWAED
RQAALRKLRY SLHQYNIVGL STNIDFLLSL SGHPQFEAGN VHTNFIPQHY DELFPTKKAT
PHEVVCQAAL GLILKEKMLT DAFRDQSDDK FSPFASSTGR RINIRYTRKL SLLDGENTVE
VAVSYNQDGS YNMQIEDKMF LISGEIFHEG DSVYLRSSVN GTVCKSKLVV LDNTIYLFFP
EGSAQIGLPV PKYLSAVSSV GTQSGAVAPM TGTVEKVFVK AGDKVQMGDP LMVMIAMKME
HTIRAPKAGV IKKVNFQEGA QANRHAPLVE FVDEEAESK
//
