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Database: UniProt
Entry: G8BT37_TETPH
LinkDB: G8BT37_TETPH
Original site: G8BT37_TETPH 
ID   G8BT37_TETPH            Unreviewed;      2317 AA.
AC   G8BT37;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCE63008.1};
GN   Name=TPHA0D03740 {ECO:0000313|EMBL:CCE63008.1};
GN   OrderedLocusNames=TPHA_0D03740 {ECO:0000313|EMBL:CCE63008.1};
OS   Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS   Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE63008.1, ECO:0000313|Proteomes:UP000005666};
RN   [1] {ECO:0000313|EMBL:CCE63008.1, ECO:0000313|Proteomes:UP000005666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC   {ECO:0000313|Proteomes:UP000005666};
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; HE612859; CCE63008.1; -; Genomic_DNA.
DR   RefSeq; XP_003685442.1; XM_003685394.1.
DR   STRING; 1071381.G8BT37; -.
DR   GeneID; 11534242; -.
DR   KEGG; tpf:TPHA_0D03740; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   HOGENOM; CLU_000395_5_1_1; -.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000005666; Chromosome 4.
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:UP000005666}.
FT   DOMAIN          144..653
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          302..494
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          780..854
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1564..1900
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1904..2219
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   2317 AA;  263501 MW;  72C47827E2D0DB89 CRC64;
     MELMSRNNIS NHSKALTSVL SRSCSKQARY YTVQNVWSSR YRYQHKLKTF GNYTIENKYY
     NRNFKRFHFN KCCRWFSSSR KHLKKALPKI RSKSFKELND PKFITNYSVK HRRLPPHFIG
     QNTIERANSS QLRDFIKIRG GHTVISKILI ANNGIAAVKM IRSIRKWAYE TFGEEKAFRF
     VVMATPEDLD ANSEYIRMAD QYVEVPGGTN NHNYANVDLI VDIAERFNVD AVWAGWGHAS
     ENQHLPEKLA QSRRKIVFIG PPSSAIRNIG DKVSSLIVAQ HAKVPCFPWS GSDIDSVKVD
     SKSGLVSVEK DLYFKACCSS PEDGLIQAKK IGFPVMIKAS EGGGGKGIRQ VRKEEDFIRL
     YHQAVNEIPG SPMFIMKLAE DVRHLEVQLL ADQYGTNITL FGRDCSVQRR HQKIIEEAPI
     TIASQAKFEK MAEAAIRLGK LVGYVSAGTV EYLYSSKEDQ AYFLELNPRL QVEHPTTEMI
     TGVNLPAAQL QIAMGIPMHR IGDIRHLYGY DAESNSVIDF SLPSKTLTEN HLKPKPKGHC
     ISCRITAEDP DQGFKPSGGL LEELNFRSSF NVWGYFSVAN KGKIHSYSDS QFGHIFAFGE
     NRQQARKRLI VSLKELSLRG EFKTTVEYLI KLLESEDFED NKISTGWLDD LISQKITSKK
     PEPILAALCA AATKAHIASK VNHEQYTESL RRGIVQPENT MLTEFQIEFL HNDFKYKFTV
     TKSSVDTYIL ELNNSKCELR VRELSDGGLL ISLGGKSHTI YWKNEVDSIR LTIDSMTTII
     KEENDPTQLR TPSPGKLVKY LVENGAHINV DEPYAEVEIM KMQMPLLAPA AGTIHILKSP
     GSTISKGELV ATLTLDDVKM ANPTLLFKGR FPNFGTAVIE GTKLAHRFQY LYYKLNNLLY
     GYDTQDSSKA ILEELLEVLR NPALPYSEWQ LQLSGLHPKI PKILDIQMQQ IVTTYSKMDS
     SFPAVELRKK LEDAINEKNS DSSMKQILEP LYDITESYLN GIKEHEYSVI IKLLGKYYDT
     ERLFIGDKVQ EEHVILKLRD ENRKNLKTVS NIVLSHSKVL RKNELVMDIL KYYYSQCHKF
     TLFTKLVEPT LINLTKLGND SNKVSLFARK LLIQCSLPSL KDKANMISSV ISRALGDSKF
     LNNIDHPQPD LKILEELIEC DFAIFDSLFP FLVNDNTPVA NAAANVYIRR AYRDFVISDL
     KFNYIERECI WSWNFKQKPE FTELFPNISS FTTESHATRE NDLSKNVFLG IEGILTYSKT
     FTELHSTITS LLAYIKSNDV KQSTTNGTIG HSKKRARILL LYVDSSSYIG NEEDVSSYFE
     SILQKHQEQL KESNITQLTL IVGNDGKLYP KYFTFNGIDC KEEKALRNTD PAMVHGLEIG
     KMAKFNISQI STGNATLHIF KGISKTLESD IRYFARGIIR KDRSINDFGS IRTYLRNKAD
     KLVNEMIDGL EVTRSEQSTL THIFLHFSDI VTLSLKDLTG TFDFLFEKYL SRLNKLKLTN
     IEIKIAIREF DKSTPLHLRI IIENPSGFVT NSQIYQEILN SEKKWIFKSI GNPGPLNMMS
     IYAPYPQITS IQQKRQKVQR LGTSYVFDFP LLFEHVVINN WKKNFPIQTL PSDMFTCCEL
     IEDASGNLVE SNRAPGNNQC GMVAFKISMK TPEYKDGRYI VIIANDLSYQ MGSFGPIEDK
     FFNNVTEYCL KHGLPRIYLS ANSGARIGIT EELVPLLNVD WKDLEDVTRG FNYLYLTESS
     FNDLKRMGKE KTVELEKITK NGEIRYIIKA IIGSSDDFGV ESLKGSGLIA GTTSRAYRDI
     FTITLVTGRS VGIGAYLVRL GQRTIQVENK PIILTGAAAI NKVLGRDVYS SNLQIGGSQI
     MYKNGISHLV SSDDLAGVES IVKWLSYIPK KRNNPVPIVN SPDSWDRDVQ YSPSSNDTYD
     IRWLIRGRTL EGIFEHGLFD KDSFFETLSG WANGVVVGRA RLGGIPVGVI GVDVRTVETV
     IPADPANPKS MESITHEAGQ VWYPNSAFKT AQTINDFNYG EQLPLIILAN WRGFSGGQQD
     MYREILKYGS FIVDSLNDYK QPVMIYIPPN GELRGGSWVV MEPSINPDHM ELYADVTSRA
     SVLEPEGMVG IKFRRNKLLK TMSQLDEQYR SLQNELLTGS LSSERYRVLA NRLQNRENEI
     MPVYKHIAAQ FFDLHDKTSR MLAKNVIKKE LVWVNSRRFL FWRLKRKLQE EYILRTMESS
     LGDSPRKDVT KLLYSWYPLD LDVEDDRSVV TWLDSNTHEV EKKVKSLKTL SMSNFLTDSI
     EKNHEESLSG ILSVLQDLPN EDKSYIIGTL TKSINKT
//
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