ID A0A1G0ZVA5_9BACT Unreviewed; 635 AA.
AC A0A1G0ZVA5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562};
GN ORFNames=A2498_07815 {ECO:0000313|EMBL:OGV62146.1};
OS Lentisphaerae bacterium RIFOXYC12_FULL_60_16.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798582 {ECO:0000313|EMBL:OGV62146.1, ECO:0000313|Proteomes:UP000178496};
RN [1] {ECO:0000313|EMBL:OGV62146.1, ECO:0000313|Proteomes:UP000178496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV62146.1}.
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DR EMBL; MHBQ01000140; OGV62146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0ZVA5; -.
DR STRING; 1798582.A2498_07815; -.
DR Proteomes; UP000178496; Unassembled WGS sequence.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR001249; AcCoA_biotinCC.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR PRINTS; PR01071; ACOABIOTINCC.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
FT DOMAIN 3..263
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 556..632
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 511..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 69170 MW; 79973EE0B0B5DD2C CRC64;
MPVRITDTTL RDAHQSLWAT RMRTADILGI VELIDQAGYY SLEVWGGATF DVCLRFLREN
PWERLRQIKS KTPKTPLQML LRGQNILGYR NYADDVLDRF IALACENGID IFRIFDALND
NRNLEHAIRS VKQHGGHAQG TLCYTISPVH TVDAYVKVAL EQVDMGIDSL CIKDMAGILS
PVAAEQLVGA LTRAIHIPVQ IHSHATSGMA PASYLEGVKA GAGAIDCAIS SMAGFSSQPP
VETMLSIFDE TPWKANLDRN ILRQICKYFA DLAPDRQPAH HPPNIIDPEI LLHHIPGGMI
SNLRSQLDQQ GALDKLDQVL EELPRTRADM GYPPLVTPTS QIVGVQAVMN ILSGERYSLV
PQETRDYVKG LYGRSPAPID PAISRKILGN EKPVTGRPAD LLGPMLPTAT RDLEPGLVQA
EEDIISYCLF PEQALEYFKW RKLPEKERPK SPADVEIEKK LEAKTPTVPP PKPLLAPSDY
LALHTLIDRI HALNFSEVTI RRQDVTLSLK AGAGDSKPTA ETTQGAPAAV ATPKAPAEPA
PSPVEPAGTN ATATDGPAIK APLNGTFYLS SGPGKPPLIK VGDVVKAGST VCIVEAMKLF
NQIKAPADAT IVQILLEHGK PVKKDQPMIV YKPAS
//
