ID A0A2T9XVW4_9CELL Unreviewed; 601 AA.
AC A0A2T9XVW4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acetyl-/propionyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:PVU84234.1};
GN ORFNames=DDP54_12150 {ECO:0000313|EMBL:PVU84234.1};
OS Cellulomonas sp. WB94.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2173174 {ECO:0000313|EMBL:PVU84234.1, ECO:0000313|Proteomes:UP000245142};
RN [1] {ECO:0000313|EMBL:PVU84234.1, ECO:0000313|Proteomes:UP000245142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB94 {ECO:0000313|EMBL:PVU84234.1,
RC ECO:0000313|Proteomes:UP000245142};
RA Anderson E., Ishii S., Jang J.;
RT "Cellulomonas - woodchip bioreactor.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVU84234.1}.
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DR EMBL; QEES01000002; PVU84234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9XVW4; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000245142; 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; 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:UP000245142}.
FT DOMAIN 1..443
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 523..600
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 508..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 601 AA; 63386 MW; 6CC321C84BABEFCB CRC64;
MSKVLIANRG EIAVRIARAC RDARIGSVAV YADTDREALH VRVADEAFAL SGARAQETYL
DIAKLLDVAR RSGADAVHPG YGFLAENADF ARAVIEAGLV WIGPPPAAIE ALGDKVSARH
IAARAGAPLV AGTPDPVTGT AEIHAFAAEH GLPVAIKAAF GGGGRGLKVA RTFDEIDEQF
ESAVREATAA FGRGECFVER FLDRPRHVET QCLADAHGTV VVVSTRDCSL QRRHQKLVEE
APAPFLTDAQ NAELVSSSVA ILREAGYVGA GTCEFLVGAD GTISFLEVNT RLQVEHPVTE
EVSGIDLVRE QLRIAAGEPL GYDHVATRGH SFEFRINGED PAAGFLPAPG RITRLRFPAG
PGVRVDSGVV EGDTVSGLFD SMIAKVIVTG STRAQAVERA RRALSELEVE GIPTVMPFHR
AVLEEADFVP ADPAEPFRVH TLWIETEFGD RLASLVAPTH ETTAGSSGAG DATDEDEDEP
IALERVIVEV GGKRLEVVLP AALGFGRGRP GNQARRPVRR QPVRSVASTN GATLSSPMQG
TIVKVAVVDG AEVAEGDLIV VLEAMKMEQP LLAHRAGRVT GLVAAVGSSV GAGTTICDIV
V
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