ID A0A423VTY4_CYTCH Unreviewed; 2283 AA.
AC A0A423VTY4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ROV94488.1};
GN ORFNames=VSDG_05901 {ECO:0000313|EMBL:ROV94488.1};
OS Cytospora chrysosperma (Cytospora canker fungus) (Sphaeria chrysosperma).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Cytosporaceae; Cytospora.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROV94488.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROV94488.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROV94488.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-biotinyl-L-lysyl-[protein] + hydrogencarbonate + ATP =
CC N(6)-carboxybiotinyl-L-lysyl-[protein] + ADP + phosphate + H(+);
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:ARBA00048600};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP +
CC phosphate + H(+); 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:ARBA00048065};
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:ROV94488.1}.
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DR EMBL; LJZO01000028; ROV94488.1; -; Genomic_DNA.
DR STRING; 252740.A0A423VTY4; -.
DR OrthoDB; 14612at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000284375; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
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 FunFam; 2.40.50.100:FF:000005; Acetyl-CoA carboxylase 1; 1.
DR FunFam; 3.30.470.20:FF:000005; Acetyl-CoA carboxylase 1; 1.
DR FunFam; 3.30.1490.20:FF:000003; acetyl-CoA carboxylase isoform X1; 1.
DR FunFam; 3.40.50.20:FF:000005; acetyl-CoA carboxylase isoform X2; 1.
DR FunFam; 3.90.226.10:FF:000010; acetyl-CoA carboxylase isoform X2; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 2.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR005479; CPAse_ATP-bd.
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:UP000284375}.
FT DOMAIN 65..573
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 222..414
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 700..774
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1523..1861
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1865..2183
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2283 AA; 255005 MW; 6D92A4FF9A88FCE8 CRC64;
MTEITNGADG GSLPRNGVVV PQSNGKASYA ELNKVADHFI GGNKLENAPD SKVKDFVAEN
DGHTVITNVL IANNGIAAVK EIRSVRKWAY ETFGDERAIQ FTVMATPEDL QANADYIRMA
DHYVEVPGGT NNHNYANVEL IVDVAERMNV HAVWAGWGHA SENPKLPESL AASPKKIVFI
GPPGSAMRSL GDKISSTIVA QHAEVPCIPW SGTGINECAV DDKGIVTVSE DVYMKGCVQS
WQEGLEKAKE IGFPVMIKAS EGGGGKGIRK ALSEEGFEQL YKQAAGEIPG SPIFIMKLAS
SARHLEVQLL ADQYGNNISL FGRDCSVQRR HQKIIEEAPV TIAKPDTFRA MEDAAVRLGK
LVGYVSAGTV EYLYSHHEDK FYFLELNPRL QVEHPTTEMV SGVNLPAAQL QIAMGLPLHR
IRDIRLLYGV DPRASTPIDF EFKNEASAKT QRRPTAKGHT TACRITSEDP GEGFKPSNGV
MHDLNFRSSS NVWGYFSVST GSGIHSFSDS QFGHIFAYGE NRQASRKHMV IALKELSIRG
DFRTTVEYLI KLLETEAFED NTITTGWLDE LISNKLTAER PDSTLAVVCG AVTKAHLASE
QCIADYKAGL NKGQVPAKDI LKTVFPVDFI YEGFRYKFTV TRSSLDTYHL FINGSKCSVG
VRALSDGGLL ILLDGRSHSV YWKEEVGATR ISVDSKTCLL EQENDPTQLR SPSPGKLVSY
SVENGEHVKA GQVFAEVEVM KMYMPLLAQE DGVVQLIKQP GATLEAGDIL GILVLDDPSR
VKQAQPFLGH LPEFGPPMVV GDKPSQRFSK LYGTLVNILE GFDNNVVMHA TLKDLIEVLR
NPELPYSEWN AQFSALHSRM PQKLDAQFSQ LVDRTKARNA EFPAKALYRT MQKFMDDNVA
PNDTAMLKST LEPLTSILDV YLEGQKVREL KVISSLIEKY AEVERLFSGK RQQDEEIILA
LRETNKDDVS NVVTTVLSHS RVSGKNNLII AILDEYRPNK PGVGNIAKYL RPVLRTLADL
ESRQTAKVSL KAREILIQCA LPSLEERKAQ MEHILRSSVV ESRYGEAGLD HRNPSLDVIK
EVVDSKYTVF DVLPQFFAHE DPWVGLAALE VYVRRAYRAY VLKKVEYHAD ESDNPAFVSW
DFKLRKIGQS EFGLPVESVA PSSPVTPATP IKAEYGFPRI NSISDMSYLT RKAEEDPLRR
GVIVPCKYLE DVEDLLAKAL ETLPTRHAKK SGLIPDLSGK RKPPVRRDSQ DELANVVNIA
IHDAQSGDDV ENLARIREII DQFKSDLIAH GVRRLTFVFG RIDGSYPAYY TFRGPSYEED
DSIRHNEPAL AFQLELNRLS KFKIKPVFTE NKNIHVYEAV AKENEADKRY FTRAVIRPGR
LRDEIPTAEY LISEADRVIN DIFDALEIIG NNNSDLNHLF INFTPVFQLQ PREVEYSLQG
FLDRFGPRGW RLRVAQVEIR IICTDPITGT PYPLRVIITN TSGFVVQVEV YAERKSEKGE
WVFHSLGGTT KIGAMHLLSV STPYPTKNHL QPKRYKAHLM GTQYVYDFPE LFRQATQNSW
AEAVKITPSM AEKQPPVGDC IDFSELVLDD TDKLTEVSRE PGTNTCGMVG WLINARTPEY
PRGRKFVVVA NDITYQIGSF GPKEDHYFNK CTELARKLGI PRIYLSANSG ARLGIATELM
PHFKIAFNDP NKQEAGFKYL YLDDDAKKRF EKTVMTEEIV EDGEKRHKIV TIVGQEDGLG
VECLRGSGLI AGATCRAYND IFTCTLVTCR SVGIGAYLVR LGQRAVQVEG QPIILTGAPA
LNNLLGREVY TSNLQLGGTQ IMYRNGVSHM VAEDDMAGIS KIVKWMSFVP DKRNNPVPIA
LTADTWDRDV VFTPAPRQPY DPRWMIGGKQ DGDDFQPGLF DKDSFVETLG GWARTVVVGR
ARLGGIPMGV IAVETRPIEN VTPADPANPD SIEQVSQEAG GVWYPNSAFK TAQAINDFNH
GEQLPLMILA NWKGFSGGQR DMYNEVLKYG SFIVDALVKY EQPIFVYIPP YGELRGGSWV
VVDPTINPAV MEMYADIEAR GGVLDPEAII GIKYRKDKQL ATMARNDPTY GALRKELAEA
QENNAPKEEM DIIHKKIADR EELLLPIYGQ ISAQFADLHD RSGRMKAKGV IRDQLEWREA
RRFFYWRVRR RLNEEYILRR MATATSQVVS TSKDPVVMRN RHLAILQAWS DIPGFDTKDR
EVALWYEENR QVVNEKVAAM KAEAARQHIT ELLMDKNAFE GVRAALSTLP IEEKEALLKQ
LSS
//
