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Database: UniProt
Entry: A0A0A8LBQ3_9SACH
LinkDB: A0A0A8LBQ3_9SACH
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ID   A0A0A8LBQ3_9SACH        Unreviewed;      2231 AA.
AC   A0A0A8LBQ3;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=WGS project CCBQ000000000 data, contig 00015 {ECO:0000313|EMBL:CDO95610.1};
GN   ORFNames=KLDO_g3844 {ECO:0000313|EMBL:CDO95610.1};
OS   Kluyveromyces dobzhanskii CBS 2104.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO95610.1, ECO:0000313|Proteomes:UP000031516};
RN   [1] {ECO:0000313|EMBL:CDO95610.1, ECO:0000313|Proteomes:UP000031516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA   Nystedt B., Astrom S.;
RT   "The genome of Kluyveromyces dobzhanskii.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC         ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC         Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC         ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00000861};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC         CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001455};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.
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:CDO95610.1}.
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DR   EMBL; CCBQ010000045; CDO95610.1; -; Genomic_DNA.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000031516; Unassembled WGS sequence.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 2.40.460.10; Biotin dependent carboxylase carboxyltransferase; 1.
DR   Gene3D; 3.90.1770.10; PreATP-grasp domain; 1.
DR   InterPro; IPR049076; ACCA.
DR   InterPro; IPR049074; ACCA_BT.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR45728:SF3; ACETYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF21385; ACCA_BT; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
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; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 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   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          59..568
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          217..409
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          695..769
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1484..1820
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1824..2139
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   2231 AA;  249229 MW;  9B63503C47FED905 CRC64;
     MSEENLSEVS VSQSKQYEIT EYGHKHSKLA SHFIGLNVVE KAEDSPLKEF VKSHGGHTVI
     SKVLIANNGI AAVKEIRSVR KWAYETFGDE RTVQFVAMAT PEDLEANAEY IRMADQYIEV
     PGGTNNNNYA NVDLILEVAE RADVDAVWAG WGHASENPLL PEKLAASKRR IIFIGPPGNA
     MRSLGDKISS TIVAQHAKVP CIPWSGTGVD KVHVDKETNL VSVEDKVYQE GCCSSPEEGL
     KKAKEIGFPI MVKASEGGGG KGIRKVENEE EFKTLYQQAA NEIPGSPIFI MKLAGKARHL
     EVQLLADQYG TNISLFGRDC SVQRRHQKII EEAPATIAKP ETFTEMEKAA VRLGQLVGYV
     SAGTVEYLYS HDDDKFYFLE LNPRLQVEHP TTEMVTGVNL PSAQLQIAMG IPMHRIRDIR
     LLYGVDPKAA SDIDFEFSAP ESVKTQRKPI PKGHCTACRI TSEDPNEGFK PSGGALHELN
     FRSSSNVWGY FSVGNNGGIH SFSDSQFGHI FAFGENRQAS RKHMVVALKE LSIRGDFRTT
     VEYLIKLLET EDFEDNTITT GWLDDLISQK MTAEKPDRTL SVICGAATKA HIASEKARED
     YISSLKRGQV PNKSLLQTMY PTEFIHDGMR YRFTVAKSAD DRYTLFINGS KCDVGVRKLS
     DGGLLIAVGG KSHTIYWKEE VSATRLSIDS KTTLLEVEND PTQLRTPSPG KLVKFLVESG
     EHVIAGQPYA EVEVMKMQMP LISQENGVAQ LLKQPGSTLI AGDILAILTL DDPSKVKHAK
     PYEGMLPELG APNVEGTKPA YKFRSLVTTL ENILKGYDNQ VIMNASLQQL IEVLRQPELP
     YSEWKLQVSA LHSRLPAKLN EQQEQLVSRS FKRGADFPAK QLEKMLEAAA NDPGVDALFG
     TTIEPLVDIT TRYCEGLAAH EHFVFATFLE NYYNVEKLFS GPNIREEDVI LKLRDENADN
     LEKVVLTVLA HSRVSARNNL ILAILKHYQP LCKLSSEVTA SIEQPLKHIV ELESKVTAKV
     ALQAREILIQ GALPSIKERT DQVQYILKSS VLSTSYGSSE TKRTKPDLEV LKDLIDSNYV
     VFDVLAQFLT NSDNAVSAAA AEVYIRRAYR AYTIGDLKHE KSSGSPVVEW KFQLPSAAFT
     SLPQVKSKLG MNRAISVSDL TYVSEGESQP LRTGLLIPSR HLDDVDGILA SALSLIPSHH
     VSTGPVPDRS GSSASLSNVA NVIVSSTEGF ESELDVLKRL REILDLNKEA LVESAIRRIT
     FVFGYSDGTY PKYYTYRGPN YKEDETIRHI EPALAFQLEL GKMSNFNIKQ IFTENRNIHV
     YEAVGKNSPV DKRFFTRGII RTGRIRDDIS ITEYLTSEAN RLMSDILDNL EIIDTSNSDL
     NHIFINFSAV FDISPEAVEA AFGGFLERFG RRLLRLRVAA AEIRIIIKDP QTGTPVPIRA
     LINNVSGFVV KTELYTEIKN AQGEWIFKSL DKPGSMHLRP IATPYPAKEW LQPKRYKAHL
     MGTTYVYDFP ELFRQAIVTQ WKKYSPKNKL SDDFFIANEL IEDENGELTE VDRELGANNI
     GMVAFKVTAK TPEYPHGRQF VIVANDITYK IGSFGPQEDA FFNKVTDYAR KRGIPRIYLS
     ANSGARIGIA EELVPLFQIA WNDEQDPSKG FQYLWLTDAA LAELKSMGKE NAVVTDRVVE
     EGKARNVITA IIGSEDGLGV ECLKGSGLIA GATSRAYKDI FTITLVTCRS VGIGAYLVRL
     GQRAIQIEAQ PIILTGAPAI NKLLGSEVYS SNLQLGGTQI MYNNGVSHLT APDDLAGVEK
     IMNWLSYIPA KRDLPVPILE SDDKWDRVVD FAPSLNEQYD VRWMIEGRKT PDGFEYGLFD
     KDSFQETLSG WAKGVVTGRA RLGGIPLGVI AVETRIVENL IPADPANPDS TEVLIQEAGQ
     VWYPNSAFKT AQAINDFNYG EQLPLMIMAN WRGFSGGQRD MYNEVLKYGS FIVDALVDYK
     QPIITYIPPT GELRGGSWVV VDPTINADQM EMYADINSRA GVLEPEGMVG IKYRREKLLA
     TMARLDDKYR ALKLKLADTN LPAEEHQEIS KQLATRERQL LPIYHQITVQ FADLHDRSGR
     MLAKGVIRKE LDWPEARRFF FWRLRRRLNE EYLMRRLNTE LASASRLEKM SRIRSWYPAS
     VSQDNDREVA TWIEENYQFL DEQVKSLKLE AFAQNLAKSI RNDRENSING LAEVLKLLST
     SDKEKLQKAL E
//
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