ID E3MCE8_CAERE Unreviewed; 2220 AA.
AC E3MCE8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=CRE-POD-2 protein {ECO:0000313|EMBL:EFO98162.1};
GN Name=Cre-pod-2 {ECO:0000313|EMBL:EFO98162.1};
GN ORFNames=CRE_15448 {ECO:0000313|EMBL:EFO98162.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) 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; DS268434; EFO98162.1; -; Genomic_DNA.
DR RefSeq; XP_003106220.1; XM_003106172.1.
DR STRING; 31234.E3MCE8; -.
DR EnsemblMetazoa; CRE15448.1; CRE15448.1; WBGene00058645.
DR GeneID; 9807788; -.
DR KEGG; crq:GCK72_025538; -.
DR CTD; 9807788; -.
DR eggNOG; KOG0368; Eukaryota.
DR HOGENOM; CLU_000395_5_2_1; -.
DR InParanoid; E3MCE8; -.
DR OMA; PTPKGHC; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000008281; 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; 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; 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:UP000008281}.
FT DOMAIN 142..642
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 299..493
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 770..845
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1483..1840
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1849..2139
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2220 AA; 248205 MW; 4DA2C1D2DFFAE9D2 CRC64;
MSHRNKDGKQ RKLPLLYGQC SQELVAKQRW NDFPDTHNGD DDDCDDVTIE LDSPTLSAIN
YAELLDALGL ALSSSICQVS LTFSGNVSDL GRSFNMSVNG HKPEFKKINL VGNAPLSDGA
VQYESIKQFV EQTVSDAEKR KPIRKLLVAT NGIAAVRCIT TINRFLNHTF RNDKLIHYVC
MATQDEIDAN SEYIKKATSL VISPSGSNKN NYANVDEVVK HAIEKKVDAV WAGWGHASEN
PDLPRRLAEN NIVFIGPPAS AMFSLGDKIA STIIAQTVGI PTIAWSGSGI TMEKTQRNKG
DFVEVPKILL EKACVRTYQE GLDALRTHNI GFPLMIKASE GGGGKGIRKC SKVEDFKSMF
VEVTLEVPNS PVFLMKCVEN ARHIEVQLIA DRYENVISVF TRDCSIQRRC QKIIEEAPAS
VAPMETRKRM QEDAVRIAKY VGYESAGTVE YLYLPEDDTY FFLELNPRLQ VEHPATEMVS
GISIPAIQIQ IAMGLPLHKI VDIRTLYNLP KSGDQELPDD VLVETAHHAI AARITSEDPD
DSFRPSTGSV KELNFNSSQD AWAYFSVSGG GKVHEFADSQ FGHLFARGTT RNQAIGNILG
ALKEMQITAS FKSQVSYLID LIQEPDFTNN GFSTQWLDDR IAKKIKQKRT LPMSDIIAIS
AAVIGYQRVT NAFETFKVSI ENGQILPPND LTETFHFDLV QDLKIYKMGV TRDHDNFVVA
LNGSQTSVNI VRFGDSGTLM ATHRESVYHC NLEEDKDIYK LKISNNIIIF EKDNDPSVLK
SPYTGKFLGY KKEEGEFVDV GEIFATVESM KLVFNVEVKK SPGRLQYVAH EGEAINPGSV
IGRLVGLENS DMYRPQQFEG TFPEWTPVKN SHPESSVNVY NECLKKCHSI LSGSNPFGGA
NEVTALVTQL FTFLNFNDLS RFILEPVLIQ VTKTFPPNVR KNFIDVVAKP CFTGDKLVQA
LNGYVLSPED RIKFDQAVNE FAYGSKGFVA GVLNNLLRAY INVEKFFEGK GYDDSVTEIK
ENNVSGDAVV QTIYSHTQIK NKNLVMRAIL ESLKQTEAKY IPSLLDNLRE IGNLHHTEEI
SSLAREILLI FQNLCYKNNY SGITASGKPA TVAEVKYWLN SPVAKRPDST GWKVIHEYFF
DKDIGSQCLD RYVAMHISAE SGYLENTYKL PTMDCTINHF SLVPKPTSFN KIVLKGNKLI
VVRLSIDSED YNTCFTNPEF LECLKKNFSQ YCKSKDVINV SIFVKILNDN SIHHDASTLT
DAEEQKVCYA QNAVVNIKAY LEKDFDVNRV NTVICLHDRP LPQLTIFEQV RLEKDRLPVN
SYPVLSRLSS VRAYQQDDAA SNFSKLFIRQ QLIIPGNKAE DVKRKVSEAV FLALDNACTA
AQVAMGKKST TGKELFFTSN HVFVFISCPG LPKEVIASEE FMTFMKECIT EEVDNHKSIL
AKHQINEVEM VYESIDGHKR IVIRDETGVT TEVITEFPET LGTYPTVSVV DKKRFAARRV
NSSYIYDFPI IFGMAAVNSW KAAESLDKDA YNKSVELLSA DMAAALNEGR WRDFFSYEEL
VFENGKLEHI SDAALLQKRS KNALNKCGMV AWTMTLYTPE KPLGYTIVLI GNDVTFQSGS
FGTAEDDLFA AASTFSREQK LPRVNVSVNS GARIGLSTKI SKLVKVQLKN DEKPDQGFDY
IYVDGEHKAD IEGQVVYEEL DNGRLKINAV IGAKNEKIGV ENLQGSGLIA GETSRAYFEV
PTYCYVTGRS VGIGAYTARL AHRIVQHKQS HLILTGYEAL NTLLGKKVYT SNNQLGGPEV
MFRNGVTHAV VENDLEGIAK VLKWMSYLPT KQNQFPYFCQ YGNDSNLRDV RVPLDGGDEK
QYDVRQLIDS KDIHNKHGIC DTMSFDEICG DWAKSIVAGR ARLCGIPIGI VASEFRNFQT
TVPADPALEG SQTQNTQRAG QVWYPDSAFK TAEAINDLNK ENLPLIIIAS LRGFSGGQKD
MYDMVLKFGA QIVDALAVYN RPVIVYIPEA GELRGGAWAV LDSKIRPEFI HLVADEKSRG
GILEPNAVVG IKFRKPVMAE MMKRCDESYA TLAADPTSKK LAEERYTELS KVYKNAAIEF
ADAHDRWQRM KSVGAVDHVT SLKNSRRLFF ALFRNELAKV GMANLYTSAP HASKPNLDFA
MNWVESNLKN SVDRSASLDE QFRQLETYSK DHLVKDVVSA VRESKRKYEE HVNNFLASCQ
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