ID A0A1H0TYK4_9PSEU Unreviewed; 649 AA.
AC A0A1H0TYK4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Propionyl-CoA carboxylase alpha chain {ECO:0000313|EMBL:SDP58845.1};
GN ORFNames=SAMN05192558_110267 {ECO:0000313|EMBL:SDP58845.1};
OS Actinokineospora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=504798 {ECO:0000313|EMBL:SDP58845.1, ECO:0000313|Proteomes:UP000199651};
RN [1] {ECO:0000313|Proteomes:UP000199651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10655 {ECO:0000313|Proteomes:UP000199651};
RA Varghese N., Submissions S.;
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; FNJB01000010; SDP58845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0TYK4; -.
DR STRING; 504798.SAMN05421871_110267; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000199651; 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; 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: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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000199651}.
FT DOMAIN 1..443
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..308
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 571..646
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 649 AA; 69034 MW; 22495FBA4541ED01 CRC64;
MITSVLVANR GEIARRVFRT ARDLGIATVA VYSDADADSP HVADADSAVR LPGNTPAETY
LRADLVIQAA RDAGADAIHP GYGFLSENAE FARAVIDAGL IWVGPPVESI ERMGSKIESK
ELMAAAGVPV LSNMDPETVT EFPVLVKASA GGGGRGMRIV RSQAELAGAV EGARSEAGSA
FGDSTVFIEP YLETGRHIEV QVMADRHGTV WAVGERECSI QRRHQKVIEE APSPLVERTE
GMRERLFDAA RKAAAAIGYE GSGTVEFLAD ESGRFFFLEM NTRLQVEHPV TECVTGLDLV
ALQLSIAEGA PLDPEPPVSR GHAIEVRLYA EDPAANWLPQ SGALHRFEIS ALASFANPPG
AGIRVDSGVV SGSLVGVHYD PMLAKVISWA PDRTSAARSL AGALLRARVH GVRTNRDLLV
RVLRHPAFLA GDTDTAFFDR HGLDTLAAPI ADKDAESLSA LAAAIADTEA NRAAAKVQGR
IPAGWRNVVS QPQVKRYESA SGEHEVRYRI TRDGLSGVEG VRLLSSSPTR VELEVAGVRR
VFDLAWYPGI ACVDSAFGSV TLTVPPRFDD PADHVAPGSL LAPMPGTVIR VAAEAGQRVD
AGQPLLWLEA MKMEHRIDAP VAGVVSELTV SPGDQVDVGR VLAVVVEES
//
