ID A0A0R3SAC4_HYMDI Unreviewed; 2635 AA.
AC A0A0R3SAC4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:VDL18756.1, ECO:0000313|WBParaSite:HDID_0000129401-mRNA-1};
GN ORFNames=HDID_LOCUS1295 {ECO:0000313|EMBL:VDL18756.1},
GN WMSIL1_LOCUS3173 {ECO:0000313|EMBL:VUZ42492.1};
OS Hymenolepis diminuta (Rat tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000129401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HDID_0000129401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL18756.1, ECO:0000313|Proteomes:UP000274504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:VUZ42492.1, ECO:0000313|Proteomes:UP000321570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMS-il1 {ECO:0000313|EMBL:VUZ42492.1,
RC ECO:0000313|Proteomes:UP000321570};
RA Jastrzebski P J., Paukszto L., Jastrzebski P J.;
RL Submitted (JUL-2019) 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}.
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DR EMBL; UYSG01000231; VDL18756.1; -; Genomic_DNA.
DR EMBL; CABIJS010000089; VUZ42492.1; -; Genomic_DNA.
DR STRING; 6216.A0A0R3SAC4; -.
DR WBParaSite; HDID_0000129401-mRNA-1; HDID_0000129401-mRNA-1; HDID_0000129401.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000046397; Unplaced.
DR Proteomes; UP000274504; Unassembled WGS sequence.
DR Proteomes; UP000321570; 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: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; 2.
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; 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:UP000274504}.
FT DOMAIN 18..527
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 174..374
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1696..2047
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 2053..2391
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 2552..2572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2615..2635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2635 AA; 293426 MW; AE62C1DED14163D8 CRC64;
MSFLSTEDFV RALDGQRCIK RILVANNGIA AVKCMRSIRS WAYVTFRNAE TFFFVCMASP
EDVHASAEYI KMANKMVMVP GGSNVNNYAN VELILQTAVS NHVDAVWAGW GHASENPQLP
EVLAKHNIAF LGPSHEAMWA LGDKIASTIL AQSAGVPTVP WSGSHITVDV KKLEKSFQYS
SLVLSELISA DDFANACVNT PEECLAVSDR IGYPVMIKAS EGGGGKGIRR VTRSEDVAGL
FNQVRSEVPE SPIFVMKCME HVRHLEVQLL ADQYGEAISL YGRDCSVQRR HQKILEEAPC
VVAPKSVFDA MERDAIRMAK LVGYCSAGTV EYLYNPRTQE YFFLELNPRL QVEHPCTEVV
SGVNLPACQL QIAMGISLIR IKDIRQLFGL AQSPILSMSL SDNLHLRHPP SSHVIAVRIT
SEDPDEGFKP HSGDVIELNF KSSRSVWGYF SVGTVGGIHE FADSQFGHCF SAEASREEAR
ENMVLALREL LIRGDFRTTV EYLIKILESD AYTRNEIDTE WLDRLIAQKD KSDKPDVLLG
VMCTALHIGY NALEKATKSF HAHVERGQFI PTNELSNIVD VTLIADGIKY VLQVVRTGKT
AFHLITNRGL QSAEVIRMSG DGLLINHDSS SYMTYCQEDA QGYRTVIDNR TVAFFKEWDP
SILRSPSTGK LVQYIVGDGC HVFENEVYAL VEVMKLVLEL RAPASGVLFH LRCVGAILEP
GAPIARLQLD DPQQCQNLEL FTGQLIPVHT SGGDTCSSSD FMVPSISSLS YGDDGVFSGI
DIICNTSGNS SSALATMISG GSAVHRVFNR CLRELEEVLL GYVLPEPFFS EWLKPKLDEL
FQCLRDPNLP LLELEDLVAQ LSGRLPICVE QQLRSIASSY SNQLTSVLAN FPSEKILRVI
EAGCPKGSKA TDSAITAYQE LTSRLVDLVR RFEGGVRGNA SRVLVNLIAA YVAVEQHYQH
GQYDRCVTLL FSRQKESTGS TGSSGGCGGS TGDLSSTATD LLPHLSGSPS CPEWITSLAD
PTVVADVVAV HFSHHHLAAK NALVCGLIER SGELREELFP RLAKDLFDSL TALTQLGQAE
NAKVALSARK FLISAQSPPY ELRRNQVESL ILSAISTFGD GNSTAENLQR LITSETSVFD
VLLEFFYHQN PNVVNAALEV YVRRAYITYE LTGLHHALIT PTSDKATIVH AIFFRFLLPN
ATMQNKLWKR AMQAKSCGSM ESDSHTSKYY IGNTEISYSP PGEKISTDFD DSDAIFNLSS
SASKACGEEF VDSTQHPDLN SWFSSDGKTP EYIRSSTDLS RQVSAVDGSE QESVPRNFSV
IDIPSHGISA EWRKQEIHNR ERLGAIVVFN SFEHMKLSFP AFMIRFEQKQ KIMMMDRRVG
GRRQGSFPTS LTCRNSIVAF QDPPFETTNA NDEPINVMNI GIRWPPEGQE EPSEEATVRM
LEGFCQEQCE RLKSVGVRRI TFMLITPGKF PLLFNYRARD DFKEDRVYRN LEPALAFQME
INRLQNYDLE PIPVLNRRMQ MYFGQAKISQ GQGAVDFRFF VRSMIRHADL VSKEASFEYL
RSEAERTLLE AMDALEMAFS HPKANFTTGN HIFLNFAPTL LLEDIAQLQS TVRSTILRYA
TRLIKLRVKQ AELKLVIRHS KNGPRIPIRL IISNEQGYSL VLELYREVPN PRTGAIHLVS
YGERKGSLHG TLASAPHQTK DFLQLKRFQA QKYSSTYVYD YPVVFRQVLG EVWKSFGGSP
PALSSCTESA NGNGRDLDAG KNLIECKELC LNSAGELVHV DRPPCLNKIG MVVWYIVMRT
PEYPEGRPMI VIANDVTHNA GSFGPCEDLV FYRASELARR LGIPRIFLAA NTGARIRLAE
EVKAAFKVAW VDEKNPVMGF NYLYLTPEDY ERLKKFNSVN CEKIVEANGE ERYKLVDIIG
KEFDISAENL RGSALIASET AQAYEKCFTL SVVTSRTIGI GAYLVRLGQR VIQIENSHII
LTGAMALNKL LGRQVYTGNG QLGGVQVMAN NGVCHLVVPD EYSAMQQVVD WLSFVPISRG
ARLPLLRGPY PDPIDRTVEY MPSRERTNDD PRWMFTGVMS GQLQTISKSP PASAEPRTDQ
TWLSGFFDRD TWREALGAWA AGVIVGRARL GGIPCGVITP ETRVSVCRVP ADPANPASEA
QTINQAGQVW YPDSSYKTAQ AIADFAREEI PLFVFANWRG FSGGLKDMYD QVLKFGAMIV
ESLRTYPTPV FIYLPPHAEL RGGAWVVIDP AINPDRMEFF CTPQTCRGGV LEPEGTVEIK
YRTPDLLSTI NRLDDQCAQL AREITAAKSA TPQSFAVVKE LQDKLKKRQQ DLLPIYHQVA
HHFADLHDTP GRLVARGLVH GIVEWRSSRA FFFARLSRRL VEQDAVQRLR RAHNPTVIPS
ASTPHQALYD PFVCRKGEQP HFNLPTVLEK PGGTTPVTGI SSANEESEIL LSTSELACKL
IAEIGAQRCV SIRQALTHIR QWFLEDNWIL NGGKSETKEL SDQDAKMTWQ QADITVARWL
AGQLGYTQLV EALRGLRNLK FDPSTCIWSL PEGDEAKQAE KTTPETSTSS FLPRLEDITR
EQIVNHIRRL LIQYPECIDE AQDCIQILQS TRPLSPSTVI GRHTSESSSE TVSKT
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