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
//