ID A0A1H8KUQ0_9ACTN Unreviewed; 736 AA.
AC A0A1H8KUQ0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Propionyl-CoA carboxylase alpha chain {ECO:0000313|EMBL:SEN96138.1};
GN ORFNames=SAMN05216267_10146 {ECO:0000313|EMBL:SEN96138.1};
OS Actinacidiphila rubida.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310780 {ECO:0000313|EMBL:SEN96138.1, ECO:0000313|Proteomes:UP000181951};
RN [1] {ECO:0000313|EMBL:SEN96138.1, ECO:0000313|Proteomes:UP000181951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2026 {ECO:0000313|EMBL:SEN96138.1,
RC ECO:0000313|Proteomes:UP000181951};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FODD01000014; SEN96138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8KUQ0; -.
DR STRING; 310780.SAMN05216267_10146; -.
DR Proteomes; UP000181951; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
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:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000181951}.
FT DOMAIN 1..442
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 114..304
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 655..731
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 448..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 76211 MW; D5DF539B41F15A4A CRC64;
MLVANRGEIA RRVFRTCRDL GITTVAVHSD ADERAPHVRE ADAAVRLPGD APADTYLRAD
LLVAAALAAG ADAVHPGYGF LSESAEFARA VQEAGLTWIG PAPGAVAAMG SKTRAKELMA
AAGVPLFGRL DPAAVTADDL PLLVKAASGG GGRGMRVVRE LDRLPAELAA AEAEACSAFG
DGEVFLEPYA EGARHVEVQV LADTHGTVWV LGERDCSLQR RHQKVIEETP APALPEDVRE
VLHEAAGRAA RSIGYTGAGT VEFLVARDGR PYFLEMNTRL QVEHPVTECV TGLDLVAWQI
RVAEGAALPP EPPRPRGHAI EARLYAEDPA RGWQPQPGPL HLLDVPGVDA EFAVPPGRET
GLRLDAGVAG GDTIGVHYDP MLAKVIAWAP TRAEAVRRLA GALERTRLHG PRTNRDLLVR
ALRHPEFAAA RLDTAFLERH SAELGVGTGA SAHADGGTST STASGTVTGT GTAADTGATS
SFVDGTAAAP EAPAQDRTAL AALAAALADA AARTAGGSAA PGAAASGPGT SGPAASGRRA
PGLSPTDSPT DGTAVAAVPI RLGGWRNVPS QPQLKRFRAE ATGAVHDVRY RLDRDGLTAP
DFPGVTLVSA APDRVVLEIA GVRHPFSVAA YAERVFVDSP FVCTALTALP RFTPPGERTA
PGSLRAPMPG TVVRIGEFTA GDRVTAGAPL LWLEAMKMEH VIAAPAAGTL TELTAEVGRQ
VELGAVLAVV KEETGP
//
