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Database: UniProt
Entry: G0WFR5_NAUDC
LinkDB: G0WFR5_NAUDC
Original site: G0WFR5_NAUDC 
ID   G0WFR5_NAUDC            Unreviewed;      2231 AA.
AC   G0WFR5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCD26626.1};
GN   Name=NDAI0I00570 {ECO:0000313|EMBL:CCD26626.1};
GN   OrderedLocusNames=NDAI_0I00570 {ECO:0000313|EMBL:CCD26626.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS   0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD26626.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD26626.1, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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}.
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DR   EMBL; HE580275; CCD26626.1; -; Genomic_DNA.
DR   RefSeq; XP_003671869.1; XM_003671821.1.
DR   STRING; 1071378.G0WFR5; -.
DR   GeneID; 11496184; -.
DR   KEGG; ndi:NDAI_0I00570; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   HOGENOM; CLU_000395_5_1_1; -.
DR   OMA; DFEDNTI; -.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000000689; Chromosome 9.
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}; Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT   DOMAIN          58..567
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          211..408
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          694..768
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1483..1819
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1823..2139
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   2231 AA;  250092 MW;  3D23AC92A0E513F8 CRC64;
     MSEENLFEET SPKQAYEITD YSSKHSKLPS HFRGLNTIDI AEESPLKEFV KSHGGHTVIS
     KILIANNGIA AVKEIRSVRK WAYETFGDDR TIQFVAMATP EDLEANAEYI RMADQYVEVP
     GGTNNNNYAN VDLIVDIAER ANVDAVWAGW GHASENPHLP EKLAKSKRKV VFIGPPGSAM
     RSLGDKISST IVAQSANVPC IPWSGTGINT VKVDKETGLV SVPDDVYQEG CCSSPEDGLV
     KAKKIGFPVM IKASEGGGGK GIRQVEREED FIPLYHQAAN EIPGSPIFIM KLAGKARHLE
     VQLLADQYGN NISLFGRDCS VQRRHQKIIE EAPVTIAPPE IFAQMEKSAV RLGQLVGYVS
     AGTVEYLYSH DEQKFYFLEL NPRLQVEHPT TEMVTGVNLP ASQLQIAMGI PMHRISDIRV
     YYGMNPHSSS EIDFEFKTEK ALKTQRKPVP KGHCTACRIT SEDPNEGFKP SGGSLHELNF
     RSSSNVWGYF SVGNNGGIHS FSDSQFGHIF AFGENRQASR KHMVVALKEL SIRGDFRTTV
     EYLIKLLETE DFEDNTITTG WLDDLISHKM TAEKPDETLA VICGATTQAF INSEKSRQKY
     IDDLKRGQVP SKSCLKTMFP VEFIHEGKRY KFTVAKSAND RYTLFINGSK CEVRARKLSD
     GGLLIALGGK SHTIYWKQEV SATRLSVDSM TTLLEVENDP TQLRTPSPGK LVKFLVENGD
     HIKAGQPYAE IEVMKMQMPL VAQESGVVQL LKQPGSTIVA GDIIAILTLD DPSKVKHALP
     FEGLLPDFGS PVVEGTKPAY KFQSLVTTLE NILQGYDNQV IMNASLQQLI EVLRDPKLPY
     SEWKLQISAL HSRLPVDLDE KLSELVDRSA KRSAVFPAKQ IAKMLDNAVK QPDTDAQLLS
     TLEPLLDITR RYTDGIEAHE HSVFVNFLEE YYDVEKLFSS ANSREESVIL KLRDENIDNL
     DKVALIVLSH AKVSAKNNLI LAILKHYQPL CKLSSHVAHI FTTPLQHLVQ LESKSTAKVA
     LQAREILIQG ALPSVKERTE QVEHILKSSV VGTTYGASNS KRTEPDLEIL KDLIDSNYVV
     FDVLIQFLNH PDPAVAAAAA QVYVRRAYRA YTVGEVRGHA STSNPVIEWK FQLPSAAFSS
     IPQMRTKMGM NRAISVSDLT YVVDSEHSPL RTGILVAADH LDDVDTNLSE SLGVIPEHAS
     TTGPVPDRSG SSSSLSNVAN IFVASTEGFE NETAILKRIR EILDVNKQDL IKSAIRRITF
     MFGCTDGSYP KYYTFNGPSY NENETIRHIE PACAFQLELG RMSNFNIKPI FTENRNIHVY
     EAVSKTSPLD KRFFTRGIIR TGRISADISI QKYLTSEANR LMSDILDNLE IIDTSNSDLN
     HIFINFSAVF DVSPEDVEAA FAGFLARFGK RYLRLRVSSA EIRIIIQDPK TGTPVPLRAL
     INNVSGYVVK SELYTEVKNN KGEWVFKSLG KPGSMHLRPI ATPYPVKEWL QPKRYKAHLM
     GTTYVYDFPD LFHQAAMSQW EKFGLETPLS DSFFIANELI EDENGELTEV EREAGVNSIG
     MVAFKVTVKT PEYPRGRQFV IVANDITYKI GSFGPQEDEF FNKVTEYARK RGIPRIYLAA
     NSGARIGIAE ELVPLYQVAW KDDKDQSKGF EYLYLTPEGM ETLKSYGKEK SVLTERVVEN
     GEERFIIKTI IGAEEGLGVE CLRGSGLIAG ATSRAYQDIF TITLVTCRSV GIGAYLVRLG
     QRAIQIEGQP IILTGAPAIN KVLGREVYSS NLQLGGTQIM YNNGVSHLTA SDDLAAVEQI
     MEWLSYIPAK RNMPVPILET EDKWDRQIDF IPRVNEPYDV RWMIEGRTLE DGGFEYGLFD
     KGSFFETLSG WAKGVVVGRA RLGGIPLGVI GVETKTIENL IPADPANPDS RESLIQEAGQ
     VWYPNSAFKT AQAIKDFNHG EQLPLMILAN WRGFSGGQRD MYNEVLKYGS FIVDALVDYK
     QPISIYIPPT GELRGGSWVV VDPTINSDQM EMYADKDSRA GVLEPEGMVG IKYRREKLLG
     TMARLDEKYK TLREKLSNKD LSVEEHQDIS KQLLIRERQL MPIYNQISIQ FADLHDRSQR
     MVSKGVIRQE LEWVEARRFF FWRLRRRLNE EYLIRRLDVE LPEAVRLEKI ARLRSWYPAS
     VDHENDRQVA TWIEDNYQLL DEHLKSLKVE SFAQGLAKKI RNDHDNVITG LSEVLKMLSS
     EDKEKILKSM K
//
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