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Database: UniProt
Entry: B3RSH2_TRIAD
LinkDB: B3RSH2_TRIAD
Original site: B3RSH2_TRIAD 
ID   B3RSH2_TRIAD            Unreviewed;      2119 AA.
AC   B3RSH2;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Acetyl-CoA carboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIADDRAFT_22916 {ECO:0000313|EMBL:EDV27057.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV27057.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV27057.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV27057.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
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; DS985243; EDV27057.1; -; Genomic_DNA.
DR   RefSeq; XP_002111053.1; XM_002111017.1.
DR   STRING; 10228.B3RSH2; -.
DR   EnsemblMetazoa; TriadT22916; TriadP22916; TriadG22916.
DR   GeneID; 6752266; -.
DR   KEGG; tad:TRIADDRAFT_22916; -.
DR   CTD; 6752266; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   HOGENOM; CLU_000395_5_0_1; -.
DR   InParanoid; B3RSH2; -.
DR   OMA; PTPKGHC; -.
DR   OrthoDB; 911at2759; -.
DR   PhylomeDB; B3RSH2; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IBA:GO_Central.
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; IBA:GO_Central.
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   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   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 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:UP000009022}.
FT   DOMAIN          16..519
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          176..367
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1465..1801
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1802..2116
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EDV27057.1"
SQ   SEQUENCE   2119 AA;  239270 MW;  5555462CE82C07FB CRC64;
     ITTPEEFVRR FGGTRAIEKV LISNNGIAAV KCMTSVRRWS YEMFGNERAI KFCSMVTPDD
     LKANAEYIKM ADHYVMVPGG TNNHNYANVD LIVEIAKRTK SQAVWAGWGH ASENPRLPEL
     LHKNDIAFIG PPEHAMWALG DKIASSIVAQ TAGVPTMPWS GSGTLKIDWV EEDVAKGKVA
     EVTDEVYKKG CVTTVDEGVN SANKIGYPVM IKASEGGGGK GIRKVESEKD FPTLFRQVQS
     EVPGSPIFIM KLAKCARHLE VQILADQYGQ AISLYGRDCS VQRRHQKIIE EAPAAIALPE
     VFRQMEKAAV TLARMVRYVS AGTVEYLYTE EDGFYFLELN PRLQVEHPCT EMVTDINLPA
     AQLQIAMGIP LHRISSIRNF YGENPLEDTP IDFSNIDKRL PPKGHVIAAR ITAENPDENF
     KPSGGMIHEL NFRSSNNVWG YFSVIASGSI HEFADSQFGH CFAWGENRED ARRNMVVALQ
     KLSIRADFRT TVEYLIKLME TDDFCNNEIS TSWLDALISK KVKAEKPDIM LAVITGALHV
     ASNDIQKRYS TYGASLERGQ VLPVNLLTNT VNVELIHDHI KYELQVTRLG LSLYAVVMNS
     SYIEVEVHRL SDSGLLISLR GNSYTTYITE EVDKYRVVIG GKTCIFEKES DPTILRSPSA
     GKLVQFLVED GGAINPTIPY AEIEARLTHY IQSLLVMKMI MSLISTESGK IHYVKRPGAI
     LEPASVLATL ELDDPNLVKK AQLFTGKFTN EQYSRLEGAQ VHQIFKASLE LLLNLMDGYC
     IPKSHFIKKL EKNIETLVSC LRDPALPLLE LKEIMHTMSG RIPASIENAI NKELAIYSSN
     ITSVLCQFPS QQIANIIDAH ASTLTKRVDR DSFFLNTQTI LQLVRRYRNG TRGHMKSVVI
     SMLKKYIEVE TIFNQGNYDK CVAALREKYS DNLSLVVTSI LSHSQVAMKN TAAVMLIDHI
     SSNETGLTDE LIAVLSELTK LNNQENAKVA LRARQVLIAA HQPSYQLRRN QVESIFLSAI
     DMHGHQFCPD NLQKLIVSET SIFDVLPSFF YHDNNIVKMA ALEVYVRRSY QAYELKSLKH
     EKLSGNKWLV EFRFLLPSSH PHRVSMNIKR TKHLSEDLSS YAAKDDSLPP CERIGAMTAI
     MIFSDLFRNF AAIIRRFRID PVSPMRSEAR KGLEPLWENQ TSHLYSDEPI HIINVAILKI
     DAYKDDALAT MLEKFVHAKK SELIEYGIRR ITILIIEEGG FPKYFTYRAN TIFQEDTIYR
     HLEPALAFQL EISRMQAFDI AYITTDNPRM HVYFGKGRKS ANESVTDRRF FIRMIIRHSD
     FVTKDASYEY LEKEGERYLL EALDTLEVLV ISPEASTDCN HIFLNFVPTV IMDPTKIEEN
     VRRMVLRYGK RLLSLRVLQA EIKMTIRLYM HADQIGLRLV LNSESGYFLS TYLYREYTDN
     RTGRVTFQSY GKVQGPMHGL SISVPYMTKD HLQSKRYQAQ QYGTTYVYDF PELFKQAVSY
     AWDEYARMNS DVTKPDVLIS CEELVLDDQG QLIVLQRLPG ENQIGMIAWK IKLFAPECPE
     GREIILIAND ITLNIGSFGL LEDEVFMKAS ELARRLGIPR IYISVNSGAR IGLAEEVKSL
     FKIAWENQNY PERGFKYLYL TPADFAKFSK AKSVKADLIE DEGESRYKIT DIIGMKDGLG
     VENLSGSGMI AGETSQAYKD IVTISLVTCR SVGIGAYLIR LGQRVIQAEN TSIILTGAQA
     LNKVLGRQVY TSNAQLGGVQ IMYHNGVSHL TVHDDFEGIY SIVKWLSFVA KSIARPLKSR
     DAVDREIGYV PSKSSFDARW MLSGKANNDG QWVSGFFDKD SFIEIQRPWA QTVIAGRARL
     GGIPVGVITA ETRAVVAEIP ADPANTESEA VILSQAGQVW YPDSSYKTAQ AINDFGREGL
     PLMIFANWRG FSGGQRDMFD EILKFGSYIV DALREYKQPI LIYIPPCGEL RGGAWVVLDP
     TINPNYMEMY ADKESRGGVL EPEGTVAIKF KKKDIIKTMN RLDANYASLS TACLNKDLKA
     EERKKLENEK LERENFLAPM YHEAAVMFAD LHDTAGRMRE KGVIREILDW KTSRRYFYWR
     LKRLLAEHEI KQLISAANP
//
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