ID A0A091ITA3_EGRGA Unreviewed; 566 AA.
AC A0A091ITA3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Propionyl-CoA carboxylase alpha chain, mitochondrial {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=Z169_03611 {ECO:0000313|EMBL:KFP11557.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP11557.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP11557.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP11557.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK500918; KFP11557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091ITA3; -.
DR STRING; 188379.A0A091ITA3; -.
DR Proteomes; UP000053119; 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 Gene3D; 3.30.700.30; -; 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; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR041265; PCC_BT.
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 Pfam; PF18140; PCC_BT; 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; PS00866; CPSASE_1; 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:UP000053119}.
FT DOMAIN 2..460
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 126..329
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP11557.1"
FT NON_TER 566
FT /evidence="ECO:0000313|EMBL:KFP11557.1"
SQ SEQUENCE 566 AA; 62604 MW; 9EAB304A1146D994 CRC64;
QTFEKLLIAN RGEIACRVIK TCKKMGIKTV AIHSDVDANA VHVKMADEAV CVGPAPTSKS
YLNMDAIMEV IKKTRAQAVS LNESICCSFS SPELISLLSL QASEGVTFIG PDTHAIQAMG
DKIESKLLAK NAKVNTIPGF DGVVKDADEA VRIAREIGYP VMIKASAGGG GKGMRIAWDD
EETREGFRFS SQEAASSFGD DRLLIEKFID NPRHIEIQVC VVIYFVVNKH GNALWLNERE
CSIQRRNQKV VEEAPSTFLD PETRRAMGEQ AVALAKAVKY SSAGTVEFLV DSSKNFYFLE
MNTRLQVEHP VTECITGLDL VQEMIRVAKG YPLRHKQADI PINGWAVECR VYAEDPYKSF
GLPSVGKLSQ YQEPLHVPSV RVDSGIQQGS DISIYYDPMI SKLITYGSNR AEALKRMEEA
LDNYVIRGVA HNISLLREVI IHPRFVQGDI STKFLPEVYP DGFKGHKLTD LERRELLATA
ASLYVAEQLR SQQFLGTPRI PIAKSKRSSW ELSVRLGDGI YPVAVSKDGS SFSVEVDGKK
LNVTSEWNLA SPLLSVTIDG TQRTIQ
//
