ID A0A1H9H4Z9_9PSEU Unreviewed; 610 AA.
AC A0A1H9H4Z9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Propionyl-CoA carboxylase alpha chain {ECO:0000313|EMBL:SEQ57424.1};
GN ORFNames=SAMN04488000_103398 {ECO:0000313|EMBL:SEQ57424.1};
OS Lentzea albida.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=65499 {ECO:0000313|EMBL:SEQ57424.1, ECO:0000313|Proteomes:UP000199503};
RN [1] {ECO:0000313|EMBL:SEQ57424.1, ECO:0000313|Proteomes:UP000199503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44437 {ECO:0000313|EMBL:SEQ57424.1,
RC ECO:0000313|Proteomes:UP000199503};
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; FOFV01000003; SEQ57424.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9H4Z9; -.
DR STRING; 65499.SAMN04488000_103398; -.
DR OrthoDB; 4435847at2; -.
DR Proteomes; UP000199503; 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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..430
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 115..305
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 533..608
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 610 AA; 65790 MW; 26173FB8D9856AF1 CRC64;
MIKSLLIANR GEIARRIIRT CRANGIRTVA VFSDPDAGSP HVREADFAVR LPGASPSETY
LRADLLVEAA VRAGADAVHP GYGFLSENAE FARKVQAAGL TWVGPEPDSI EAMGSKVAAK
KRMAAAGVPT LPELDPETVT EFPVLIKASA GGGGRGMRIV REKGEFADAL ASARREAESA
FGDPTVFCEP LLEQARHVEV QVLADAHGTV WALGERECSI QRRHQKIVEE SPSPAVGDEV
RTRLFAAATA AAESIGYVGA GTVEFMLKGE DFHFLEVNTR LQVEHPVTEL VYGVDLVEWQ
LRIAEGARLP ADVPEPRGHA IEVRLYAEDP ANDWRPASGT LHRFEVPGDV RLDSGVEDGS
VVSVHYDPML AKVIAYAPTR RAAARKLATA LESARIHGLI TNRQLLVDIL GNEAFLDGET
HTGFLTEHDF TRTVDPQPFA RAAALASAAT RRIGTLPLGW RNVRSQQPKA KFLHGDELVE
VEYDPREATA DTVVLDLDGV RVPFHVSRYG DVVEVDSPRG SVSLKVVPRF PEPETKLAPG
ATVAPMPGTV VRVSVQQGDQ VEAGAELLVL EAMKMEHRVL ATNAGTVIEL LVEQAQQVNA
GDVLAVVEES
//
