ID A0A8B9VS05_9AVES Unreviewed; 606 AA.
AC A0A8B9VS05;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Propionyl-CoA carboxylase subunit alpha {ECO:0000313|Ensembl:ENSAZOP00000025234.1};
OS Anas zonorhyncha (Eastern spot-billed duck).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=75864 {ECO:0000313|Ensembl:ENSAZOP00000025234.1, ECO:0000313|Proteomes:UP000694549};
RN [1] {ECO:0000313|Ensembl:ENSAZOP00000025234.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSAZOP00000025234.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR AlphaFoldDB; A0A8B9VS05; -.
DR Ensembl; ENSAZOT00000027067.1; ENSAZOP00000025234.1; ENSAZOG00000010367.1.
DR Proteomes; UP000694549; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:TreeGrafter.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR FunFam; 3.30.1490.20:FF:000003; acetyl-CoA carboxylase isoform X1; 1.
DR FunFam; 3.30.470.20:FF:000028; Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; 1.
DR FunFam; 3.40.50.20:FF:000010; Propionyl-CoA carboxylase subunit alpha; 1.
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; IPR050856; Biotin_carboxylase_complex.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CPAse_ATP-bd.
DR InterPro; IPR041265; PCC_BT.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; NF006367; PRK08591.1; 1.
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 Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000694549}.
FT DOMAIN 45..492
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 164..361
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 606 AA; 67328 MW; E211BF879A07C16C CRC64;
MAAALGGAAR GRLRALLECE TLCLRWYLKT SHKLYSVTYD PNEKTFEKLL IANRGEIACR
VIKTCKKMGI KTVAIHSDVD ANAVHVKMAD EAVCVGPAPT SKSYLNMDAI MEVIKETRAQ
AVHPGYGFLS ENKEFARRLA AEGVTFIGPD THAIQAMGDK IESKLLAKNA KVNTIPGFDG
VVKDADEAVR IAREIGYPVM IKASAGGGGK GMRIAWDDEE TREGFRFSSQ EAASSFGDDR
LLIEKFIDNP RHIEIQVLAD KHGNALWLNE RECSIQRRNQ KVVEEAPSTF LDPETRRAMG
EQAVALAKAV KYSSAGTVEF LVDSSKNFYF LEMNTRLQVE HPVTECITGL DLVQEMIRVA
KGYPLRHKQA DIPINGWAVE CRVYAEDPYK SFGLPSIGKL SQYQEPLHVP SVRVDSGIQQ
GSDISIYYDP MISKLITYGS NRAEALKRME EALDNYVIRG VTHNISLLRE VIIHPRFVRG
DISTKFLPEV YPDGFKGHKL TDLERRELLA TAASLYVAEQ LRSQRFLGTP RIPIAKSKRS
SWELSVHLGD GIYPVAVSKD GSSFSVEVDG MKLNVTSEWN LASPLLSVTI DGTQRTIQVN
SPMLYL
//
