ID F9FUQ0_FUSOF Unreviewed; 398 AA.
AC F9FUQ0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Pyruvate carboxyltransferase domain-containing protein {ECO:0000259|PROSITE:PS50991};
GN ORFNames=FOXB_10131 {ECO:0000313|EMBL:EGU79348.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU79348.1};
RN [1] {ECO:0000313|EMBL:EGU79348.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU79348.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
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:EGU79348.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFQF01002685; EGU79348.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FUQ0; -.
DR STRING; 660025.F9FUQ0; -.
DR PaxDb; 5507-FOXG_01149P0; -.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR CDD; cd07948; DRE_TIM_HCS; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR048253; DRE_TIM_HCS_fun_bact.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR10277:SF48; HOMOCITRATE SYNTHASE, CYTOSOLIC ISOZYME-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 120..373
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 42100 MW; E605548D0DF69967 CRC64;
MQSANNPISH HTSHTMGQGA ASSNGGDNSC GANCVDNHVG HAIGDGDGVV RVSGGETGND
GGHVVEASVT DVGVNDLNQT TTTYDESDDE SSLADSSGSI SDGPSFGGTS IRSLGSMSNF
SIIDTTLREG EQFINGNYDT ETKLKIARAL DDIGVEYIEV TSPAASPQSK LDCAAICKLG
LKAKVLCHIR CNMDDARTAV ETGVDGINMC IGTSTQLMEH SHGKDLDWIA AKAKEVIEFT
QAHGIEVRFS GEDSFRSDFS EILKLYSLMD RLGAHRVGIA DTVGGATPRE VFDKISTLKQ
MVGCDIETHF HNDTGCAVAN AYTAIEAGAT HIDTTVLGIG ERNGITSLSK LLQCMLQMGH
DSVLAKYKLE KIPALEQLVA EAVNIEIPWN NASLAAYL
//
