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
//