ID A0A2H5NNG9_CITUN Unreviewed; 2255 AA.
AC A0A2H5NNG9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAY41652.1};
GN ORFNames=CUMW_061090 {ECO:0000313|EMBL:GAY41652.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY41652.1, ECO:0000313|Proteomes:UP000236630};
RN [1] {ECO:0000313|EMBL:GAY41652.1, ECO:0000313|Proteomes:UP000236630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Miyagawa wase {ECO:0000313|Proteomes:UP000236630};
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAY41652.1}.
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DR EMBL; BDQV01000014; GAY41652.1; -; Genomic_DNA.
DR STRING; 55188.A0A2H5NNG9; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000236630; 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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000236630}.
FT DOMAIN 77..584
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 230..422
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 711..785
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1535..1873
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1877..2192
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2093..2132
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2255 AA; 251703 MW; 7113B8B11A295735 CRC64;
MALALSSQQG CSAEGSKQLR REEERSGEGS MSEAQRRSAM AGLGRGNGHI NGAVPIRSPA
AMSEVDEFCR SLGGKKPIHS ILIANNGMAA VKFIRSIRTW AYETFGTEKA ILLVAMATPE
DMRINAEHIR IADQFVEVPG GTNNNNYANV QLIVEMAEMT RVDAVWPGWG HASEIPELPD
TLSTKGIIFL GPPATSMAAL GDKIGSSLIA QAADVPTLLW SGSHVKIPPE SCLVTIPDDV
YRQACVYTTE EAIASCQVVG YPAMIKASWG GGGKGIRKVH NDDEVRALFK QVQGEVPGSP
IFIMKVASQS RHLEVQLLCD QYGNVAALHS RDCSVQRRHQ KIIEEGPITV APLETVKKLE
QAARRLAKCV NYVGAATVEY LYSMETGEYY FLELNPRLQV EHPVTEWIAE INLPAAQVAV
GMGIPLWQIP EIRRFYGMEH GGGYDAWRKT SVIATPFDFD QAESTRPKGH CVAVRVTSED
PDDGFKPTSG KVQELSFKSK PNVWAYFSVK SGGGIHEFSD SQFGHVFAFG ESRALAIANM
VLGLKEIQIR GEIRTNVDYT IDLLHASDYR ENKIHTGWLD SRIAMRVRAE RPPWYLSVVG
GALYKASASS AAMVSDYIGY LEKGQIPPKH ISLVNSQVSL NIEGSKYRID MVRRGPGSYT
LRMNESEIEA EIHTLRDGGL LMQLDGNSHI VYAEEEAAGT RLLIDGRTCL LQNDHDPSKL
VAETPCKLLR YLVSDGSHID ADTPYAEVEV MKMCMPLLSP ASGVLQFKMA EGQAMQAGEL
IARLDLDDPS AVRKAEPFYG SFPILGPPTA ISGKVHQRCA ASLNAARMIL AGYEHNIEEV
VQNLLNCLDS PELPFLQWQE CMAVLSTRLP KDLKNQLESK FKEFERISSS QNVDFPAKLL
RGVLEAHLLS CADKERGSQE RLIEPLMSLV KSYEGGRESH ARVIVQSLFE EYLSVEELFS
DQIQADVIER LRLQYQKDLL KVVDIVLSHQ GVKRKNKLIL RLMEQLVYPN PAAYRDKLIR
FSALNHTNYS ELALKASQLL EQTKLSELRS SIARSLSELE MFTEDGESMD TPKRKSAIDE
RMEDLVSAPL AVEDALVGLF DHSDHTLQRR VVETYVRRLY QPYLVKGSVR MQWHRCGLIA
SWEFLEEHIE RKNGPEDQTP EQPLVEKHSE RKWGAMVIIK SLQSFPDILS AALRETAHSR
NDSIWKGSAQ TASYGNMMHI ALVGMNNQMS LLQDSGDEDQ AQERINKLAK ILKEQEVGSG
LHSAGVGVIS CIIQRDEGRA PMRHSFHWSP EKFYYEEEPL LRHLEPPLSI YLELDKLKGY
DNIQYTLSRD RQWHLYTVVD KPLPIRRMFL RTLVRQPTSN EGFMSYPVSD MGTNRAQWTM
SFTSRGVLRS LMAAMEELEL NVHNASVKSD HAQMYLCILR EQKINDLVPY PKRVDVDAGQ
EETAIEALLE ELAREIHATV GVRMHKLGVC EWEVKLWMAS SGQANGAWRV VVTNVTGHTC
AVHIYRELED TSKHTVVYHS VAVRGLLHGV EVNAQYQSLG VLDQKRLLAR RSNTTYCYDF
PLAFETALEQ SWASQFPNMR PKDKALLKVT ELKFADDSGT WGTPLVLVER SPGLNNIGMV
AWCMEMFTPE FPSGRTILIV ANDVTFKAGS FGPREDAFFL AVTDLACAKK LPLIYLAANS
GARIGVAEEV KACFKIGWTD ELNPDRGFNY VYLTPEDYVR IGSSVIAHEM KLESGETRWV
VDSIVGKEDG LGVENLTGSG AIAGAYSRAY KETFTLTYVT GRTVGIGAYL ARLGMRCIQR
LDQPIILTGF SALNKLLGRE VYSSHMQLGG PKIMATNGVV HLTVSDDLEG ISAILKWLSY
VPPHIGGALP IISPLDPPDR PVEYLPENSC DPRAAICGSL DNNGKWIGGI FDKDSFVETL
EGWARTVVTG RARLGGIPVG IVAVETQTVM QVIPADPGQL DSHERVVPQA GQVWFPDSAT
KTAQALMDFN REELPLFILA NWRGFSGGQR DLFEGILQAG STIVENLRTY KQPVFVYIPM
MAELRGGAWV VVDSRINSDH IEMYADRTAK GNVLEPEGMI EIKFRTKELL ECMGRLDQKL
IDLRAKLQEA KNNRTLAMVE SLQQQIKARE KQLLPTYTQV ATKFAELHDT SLRMAAKGVI
KEVVDWDKSR SFFCRRLRRR VAESSLVKTL TAAAGDYLSH KSAIEMIKQW FLDSEIARGK
EGAWLDDETF FTWKDDSRNY EKKVQELGVQ KCRLS
//
